2bfb - Revision history

OCA at 13:32, 13 December 2023

2023-12-13T13:32:14Z

← Older revision		Revision as of 13:32, 13 December 2023
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	<StructureSection load='2bfb' size='340' side='right'caption='[[2bfb]], [[Resolution\|resolution]] 1.77Å' scene=''>		<StructureSection load='2bfb' size='340' side='right'caption='[[2bfb]], [[Resolution\|resolution]] 1.77Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2bfb]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Human Human~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BFB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BFB FirstGlance]. <br>		<table><tr><td colspan='2'>[[2bfb]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BFB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BFB FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=MRD:(4R)-2-METHYLPENTANE-2,4-DIOL'>MRD</scene>, <scene name='pdbligand=TPP:THIAMINE+DIPHOSPHATE'>TPP</scene~~></td></tr>~~		</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution\|Resolution]] 1.77Å</td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1dtw\|1dtw]], [[1ols\|1ols]], [[1olu\|1olu]], [[1olx\|1olx]], [[1u5b\|1u5b]], [[1v11\|1v11]], [[1v16\|1v16]], [[1v1m\|1v1m]], [[1v1r\|1v1r]], [[1wci\|1wci]], [[1x7w\|1x7w]], [[1x7x\|1x7x]], [[1x7y\|1x7y]], [[1x7z\|1x7z]], [[1x80\|1x80]], [[2beu\|2beu]], [[2bev\|2bev]], [[2bew\|2bew]], [[2bfc\|2bfc]], [[2bfd\|2bfd]], [[2bfe\|2bfe]], [[2bff\|2bff]]</div></td></tr>		<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=MRD:(4R)-2-METHYLPENTANE-2,4-DIOL'>MRD</scene>, <scene name='pdbligand=TPP:THIAMINE+DIPHOSPHATE'>TPP</scene></td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/3-methyl-2-oxobutanoate_dehydrogenase_(2-methylpropanoyl-transferring) 3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring)], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.2.4.4 1.2.4.4] </span></td></tr>
	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2bfb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bfb OCA], [https://pdbe.org/2bfb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2bfb RCSB], [https://www.ebi.ac.uk/pdbsum/2bfb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2bfb ProSAT]</span></td></tr>		<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2bfb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bfb OCA], [https://pdbe.org/2bfb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2bfb RCSB], [https://www.ebi.ac.uk/pdbsum/2bfb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2bfb ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
	[[https://www.uniprot.org/uniprot/ODBA_HUMAN ODBA_HUMAN]] Defects in BCKDHA are a cause of maple syrup urine disease type IA (MSUD1A) [MIM:[https://omim.org/entry/248600 248600]]. MSUD is an autosomal recessive disorder characterized by mental and physical retardation, feeding problems, and a maple syrup odor to the urine.<ref>PMID:2060625</ref> <ref>PMID:8037208</ref> <ref>PMID:2703538</ref> <ref>PMID:2241958</ref> <ref>PMID:1867199</ref> <ref>PMID:1885764</ref> <ref>PMID:8161368</ref> <ref>PMID:7883996</ref> [[https://www.uniprot.org/uniprot/ODBB_HUMAN ODBB_HUMAN]] Defects in BCKDHB are the cause of maple syrup urine disease type IB (MSUD1B) [MIM:[https://omim.org/entry/248600 248600]]. MSUD is an autosomal recessive disorder characterized by mental and physical retardation, feeding problems, and a maple syrup odor to the urine.<ref>PMID:8161368</ref> <ref>PMID:11509994</ref> <ref>PMID:22326532</ref>		[https://www.uniprot.org/uniprot/ODBA_HUMAN ODBA_HUMAN] Defects in BCKDHA are a cause of maple syrup urine disease type IA (MSUD1A) [MIM:[https://omim.org/entry/248600 248600]. MSUD is an autosomal recessive disorder characterized by mental and physical retardation, feeding problems, and a maple syrup odor to the urine.<ref>PMID:2060625</ref> <ref>PMID:8037208</ref> <ref>PMID:2703538</ref> <ref>PMID:2241958</ref> <ref>PMID:1867199</ref> <ref>PMID:1885764</ref> <ref>PMID:8161368</ref> <ref>PMID:7883996</ref>
	== Function ==		== Function ==
	[[https://www.uniprot.org/uniprot/ODBA_HUMAN ODBA_HUMAN]] The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO(2). It contains multiple copies of three enzymatic components: branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3). [[https://www.uniprot.org/uniprot/ODBB_HUMAN ODBB_HUMAN]] The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO(2). It contains multiple copies of three enzymatic components: branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3).		[https://www.uniprot.org/uniprot/ODBA_HUMAN ODBA_HUMAN] The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO(2). It contains multiple copies of three enzymatic components: branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3).
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
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	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: ~~Human~~]]		[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
	[[Category: Brautigam~~, C A~~]]		[[Category: Brautigam CA]]
	[[Category: Chuang~~, D T~~]]		[[Category: Chuang DT]]
	[[Category: Chuang~~, J L~~]]		[[Category: Chuang JL]]
	[[Category: Machius, M]]		[[Category: Machius M]]
	[[Category: Tomchick~~, D R~~]]		[[Category: Tomchick DR]]
	[[Category: Wynn~~, R M]]~~		[[Category: Wynn RM]]
	~~[[Category: Acylation]]~~
	~~[[Category: Maple syrup urine disease]]~~
	~~[[Category: Multi-enzyme complex]]~~
	~~[[Category: Oxidative decarboxylation]]~~
	~~[[Category: Oxidoreductase]]~~
	~~[[Category: Phosphorylation]]~~
	~~[[Category: Thiamine diphosphate~~]]

OCA at 10:23, 4 August 2021

2021-08-04T10:23:36Z

← Older revision		Revision as of 10:23, 4 August 2021
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	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2bfb]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BFB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BFB FirstGlance]. <br>		<table><tr><td colspan='2'>[[2bfb]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BFB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BFB FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=MRD:(4R)-2-METHYLPENTANE-2,4-DIOL'>MRD</scene>, <scene name='pdbligand=~~TDP~~:~~THIAMIN~~+DIPHOSPHATE'>~~TDP~~</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=MRD:(4R)-2-METHYLPENTANE-2,4-DIOL'>MRD</scene>, <scene name='pdbligand=TPP:THIAMINE+DIPHOSPHATE'>TPP</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1dtw\|1dtw]], [[1ols\|1ols]], [[1olu\|1olu]], [[1olx\|1olx]], [[1u5b\|1u5b]], [[1v11\|1v11]], [[1v16\|1v16]], [[1v1m\|1v1m]], [[1v1r\|1v1r]], [[1wci\|1wci]], [[1x7w\|1x7w]], [[1x7x\|1x7x]], [[1x7y\|1x7y]], [[1x7z\|1x7z]], [[1x80\|1x80]], [[2beu\|2beu]], [[2bev\|2bev]], [[2bew\|2bew]], [[2bfc\|2bfc]], [[2bfd\|2bfd]], [[2bfe\|2bfe]], [[2bff\|2bff]]</div></td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1dtw\|1dtw]], [[1ols\|1ols]], [[1olu\|1olu]], [[1olx\|1olx]], [[1u5b\|1u5b]], [[1v11\|1v11]], [[1v16\|1v16]], [[1v1m\|1v1m]], [[1v1r\|1v1r]], [[1wci\|1wci]], [[1x7w\|1x7w]], [[1x7x\|1x7x]], [[1x7y\|1x7y]], [[1x7z\|1x7z]], [[1x80\|1x80]], [[2beu\|2beu]], [[2bev\|2bev]], [[2bew\|2bew]], [[2bfc\|2bfc]], [[2bfd\|2bfd]], [[2bfe\|2bfe]], [[2bff\|2bff]]</div></td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/3-methyl-2-oxobutanoate_dehydrogenase_(2-methylpropanoyl-transferring) 3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring)], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.2.4.4 1.2.4.4] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/3-methyl-2-oxobutanoate_dehydrogenase_(2-methylpropanoyl-transferring) 3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring)], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.2.4.4 1.2.4.4] </span></td></tr>

OCA at 10:31, 17 February 2021

2021-02-17T10:31:27Z

OCA at 11:49, 10 May 2019

2019-05-10T11:49:52Z

← Older revision		Revision as of 11:49, 10 May 2019
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	==Reactivity modulation of human branched-chain alpha-ketoacid dehydrogenase by an internal molecular switch==		==Reactivity modulation of human branched-chain alpha-ketoacid dehydrogenase by an internal molecular switch==
	<StructureSection load='2bfb' size='340' side='right' caption='[[2bfb]], [[Resolution\|resolution]] 1.77Å' scene=''>		<StructureSection load='2bfb' size='340' side='right'caption='[[2bfb]], [[Resolution\|resolution]] 1.77Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2bfb]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BFB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2BFB FirstGlance]. <br>		<table><tr><td colspan='2'>[[2bfb]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BFB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2BFB FirstGlance]. <br>
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	==See Also==		==See Also==
	*[[2-oxoisovalerate dehydrogenase\|2-oxoisovalerate dehydrogenase]]		*[[2-oxoisovalerate dehydrogenase 3D structures\|2-oxoisovalerate dehydrogenase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
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	</StructureSection>		</StructureSection>
	[[Category: Human]]		[[Category: Human]]
			[[Category: Large Structures]]
	[[Category: Brautigam, C A]]		[[Category: Brautigam, C A]]
	[[Category: Chuang, D T]]		[[Category: Chuang, D T]]

OCA at 07:45, 6 March 2019

2019-03-06T07:45:04Z

← Older revision		Revision as of 07:45, 6 March 2019
Line 1:		Line 1:

	==Reactivity modulation of human branched-chain alpha-ketoacid dehydrogenase by an internal molecular switch==		==Reactivity modulation of human branched-chain alpha-ketoacid dehydrogenase by an internal molecular switch==
	<StructureSection load='2bfb' size='340' side='right' caption='[[2bfb]], [[Resolution\|resolution]] 1.77Å' scene=''>		<StructureSection load='2bfb' size='340' side='right' caption='[[2bfb]], [[Resolution\|resolution]] 1.77Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2bfb]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BFB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2BFB FirstGlance]. <br>		<table><tr><td colspan='2'>[[2bfb]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BFB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2BFB FirstGlance]. <br>
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	</div>		</div>
	<div class="pdbe-citations 2bfb" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 2bfb" style="background-color:#fffaf0;"></div>

			==See Also==
			*[[2-oxoisovalerate dehydrogenase\|2-oxoisovalerate dehydrogenase]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 06:20, 16 May 2018

2018-05-16T06:20:08Z

← Older revision		Revision as of 06:20, 16 May 2018
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	==~~REACTIVITY MODULATION OF HUMAN BRANCHED~~-~~CHAIN ALPHA~~-~~KETOACID DEHYDROGENASE BY AN INTERNAL MOLECULAR SWITCH~~==
			==Reactivity modulation of human branched-chain alpha-ketoacid dehydrogenase by an internal molecular switch==
	<StructureSection load='2bfb' size='340' side='right' caption='[[2bfb]], [[Resolution\|resolution]] 1.77Å' scene=''>		<StructureSection load='2bfb' size='340' side='right' caption='[[2bfb]], [[Resolution\|resolution]] 1.77Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
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	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1dtw\|1dtw]], [[1ols\|1ols]], [[1olu\|1olu]], [[1olx\|1olx]], [[1u5b\|1u5b]], [[1v11\|1v11]], [[1v16\|1v16]], [[1v1m\|1v1m]], [[1v1r\|1v1r]], [[1wci\|1wci]], [[1x7w\|1x7w]], [[1x7x\|1x7x]], [[1x7y\|1x7y]], [[1x7z\|1x7z]], [[1x80\|1x80]], [[2beu\|2beu]], [[2bev\|2bev]], [[2bew\|2bew]], [[2bfc\|2bfc]], [[2bfd\|2bfd]], [[2bfe\|2bfe]], [[2bff\|2bff]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1dtw\|1dtw]], [[1ols\|1ols]], [[1olu\|1olu]], [[1olx\|1olx]], [[1u5b\|1u5b]], [[1v11\|1v11]], [[1v16\|1v16]], [[1v1m\|1v1m]], [[1v1r\|1v1r]], [[1wci\|1wci]], [[1x7w\|1x7w]], [[1x7x\|1x7x]], [[1x7y\|1x7y]], [[1x7z\|1x7z]], [[1x80\|1x80]], [[2beu\|2beu]], [[2bev\|2bev]], [[2bew\|2bew]], [[2bfc\|2bfc]], [[2bfd\|2bfd]], [[2bfe\|2bfe]], [[2bff\|2bff]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/3-methyl-2-oxobutanoate_dehydrogenase_(2-methylpropanoyl-transferring) 3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.2.4.4 1.2.4.4] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/3-methyl-2-oxobutanoate_dehydrogenase_(2-methylpropanoyl-transferring) 3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.2.4.4 1.2.4.4] </span></td></tr>
	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2bfb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bfb OCA], [http://pdbe.org/2bfb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2bfb RCSB], [http://www.ebi.ac.uk/pdbsum/2bfb PDBsum]</span></td></tr>		<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2bfb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bfb OCA], [http://pdbe.org/2bfb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2bfb RCSB], [http://www.ebi.ac.uk/pdbsum/2bfb PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2bfb ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
Line 16:		Line 17:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bf/2bfb_consurf.spt"</scriptWhenChecked>		<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bf/2bfb_consurf.spt"</scriptWhenChecked>
	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>		<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
	</jmolCheckbox>		</jmolCheckbox>
	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/~~chain_selection~~.php?pdb_ID=~~2ata~~ ConSurf].		</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2bfb ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">

OCA at 12:00, 11 September 2015

2015-09-11T12:00:16Z

← Older revision		Revision as of 12:00, 11 September 2015
Line 2:		Line 2:
	<StructureSection load='2bfb' size='340' side='right' caption='[[2bfb]], [[Resolution\|resolution]] 1.77Å' scene=''>		<StructureSection load='2bfb' size='340' side='right' caption='[[2bfb]], [[Resolution\|resolution]] 1.77Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2bfb]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Homo_sapiens Homo sapiens~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BFB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2BFB FirstGlance]. <br>		<table><tr><td colspan='2'>[[2bfb]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BFB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2BFB FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=MRD:(4R)-2-METHYLPENTANE-2,4-DIOL'>MRD</scene>, <scene name='pdbligand=TDP:THIAMIN+DIPHOSPHATE'>TDP</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=MRD:(4R)-2-METHYLPENTANE-2,4-DIOL'>MRD</scene>, <scene name='pdbligand=TDP:THIAMIN+DIPHOSPHATE'>TDP</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1dtw\|1dtw]], [[1ols\|1ols]], [[1olu\|1olu]], [[1olx\|1olx]], [[1u5b\|1u5b]], [[1v11\|1v11]], [[1v16\|1v16]], [[1v1m\|1v1m]], [[1v1r\|1v1r]], [[1wci\|1wci]], [[1x7w\|1x7w]], [[1x7x\|1x7x]], [[1x7y\|1x7y]], [[1x7z\|1x7z]], [[1x80\|1x80]], [[2beu\|2beu]], [[2bev\|2bev]], [[2bew\|2bew]], [[2bfc\|2bfc]], [[2bfd\|2bfd]], [[2bfe\|2bfe]], [[2bff\|2bff]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1dtw\|1dtw]], [[1ols\|1ols]], [[1olu\|1olu]], [[1olx\|1olx]], [[1u5b\|1u5b]], [[1v11\|1v11]], [[1v16\|1v16]], [[1v1m\|1v1m]], [[1v1r\|1v1r]], [[1wci\|1wci]], [[1x7w\|1x7w]], [[1x7x\|1x7x]], [[1x7y\|1x7y]], [[1x7z\|1x7z]], [[1x80\|1x80]], [[2beu\|2beu]], [[2bev\|2bev]], [[2bew\|2bew]], [[2bfc\|2bfc]], [[2bfd\|2bfd]], [[2bfe\|2bfe]], [[2bff\|2bff]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/3-methyl-2-oxobutanoate_dehydrogenase_(2-methylpropanoyl-transferring) 3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.2.4.4 1.2.4.4] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/3-methyl-2-oxobutanoate_dehydrogenase_(2-methylpropanoyl-transferring) 3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.2.4.4 1.2.4.4] </span></td></tr>
	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2bfb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bfb OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2bfb RCSB], [http://www.ebi.ac.uk/pdbsum/2bfb PDBsum]</span></td></tr>		<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2bfb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bfb OCA], [http://pdbe.org/2bfb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2bfb RCSB], [http://www.ebi.ac.uk/pdbsum/2bfb PDBsum]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
Line 30:		Line 30:
	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
			<div class="pdbe-citations 2bfb" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: ~~Homo sapiens~~]]		[[Category: Human]]
	[[Category: Brautigam, C A]]		[[Category: Brautigam, C A]]
	[[Category: Chuang, D T]]		[[Category: Chuang, D T]]

OCA at 09:05, 8 January 2015

2015-01-08T09:05:14Z

← Older revision		Revision as of 09:05, 8 January 2015
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2bfb]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BFB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2BFB FirstGlance]. <br>		<table><tr><td colspan='2'>[[2bfb]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BFB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2BFB FirstGlance]. <br>
	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=MRD:(4R)-2-METHYLPENTANE-2,4-DIOL'>MRD</scene>, <scene name='pdbligand=TDP:THIAMIN+DIPHOSPHATE'>TDP</scene><br>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=MRD:(4R)-2-METHYLPENTANE-2,4-DIOL'>MRD</scene>, <scene name='pdbligand=TDP:THIAMIN+DIPHOSPHATE'>TDP</scene></td></tr>
	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1dtw\|1dtw]], [[1ols\|1ols]], [[1olu\|1olu]], [[1olx\|1olx]], [[1u5b\|1u5b]], [[1v11\|1v11]], [[1v16\|1v16]], [[1v1m\|1v1m]], [[1v1r\|1v1r]], [[1wci\|1wci]], [[1x7w\|1x7w]], [[1x7x\|1x7x]], [[1x7y\|1x7y]], [[1x7z\|1x7z]], [[1x80\|1x80]], [[2beu\|2beu]], [[2bev\|2bev]], [[2bew\|2bew]], [[2bfc\|2bfc]], [[2bfd\|2bfd]], [[2bfe\|2bfe]], [[2bff\|2bff]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1dtw\|1dtw]], [[1ols\|1ols]], [[1olu\|1olu]], [[1olx\|1olx]], [[1u5b\|1u5b]], [[1v11\|1v11]], [[1v16\|1v16]], [[1v1m\|1v1m]], [[1v1r\|1v1r]], [[1wci\|1wci]], [[1x7w\|1x7w]], [[1x7x\|1x7x]], [[1x7y\|1x7y]], [[1x7z\|1x7z]], [[1x80\|1x80]], [[2beu\|2beu]], [[2bev\|2bev]], [[2bew\|2bew]], [[2bfc\|2bfc]], [[2bfd\|2bfd]], [[2bfe\|2bfe]], [[2bff\|2bff]]</td></tr>
	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/3-methyl-2-oxobutanoate_dehydrogenase_(2-methylpropanoyl-transferring) 3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.2.4.4 1.2.4.4] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/3-methyl-2-oxobutanoate_dehydrogenase_(2-methylpropanoyl-transferring) 3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.2.4.4 1.2.4.4] </span></td></tr>
	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2bfb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bfb OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2bfb RCSB], [http://www.ebi.ac.uk/pdbsum/2bfb PDBsum]</span></td></tr>		<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2bfb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bfb OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2bfb RCSB], [http://www.ebi.ac.uk/pdbsum/2bfb PDBsum]</span></td></tr>
	<table>		</table>
	== Disease ==		== Disease ==
	[[http://www.uniprot.org/uniprot/ODBA_HUMAN ODBA_HUMAN]] Defects in BCKDHA are a cause of maple syrup urine disease type IA (MSUD1A) [MIM:[http://omim.org/entry/248600 248600]]. MSUD is an autosomal recessive disorder characterized by mental and physical retardation, feeding problems, and a maple syrup odor to the urine.<ref>PMID:2060625</ref> <ref>PMID:8037208</ref> <ref>PMID:2703538</ref> <ref>PMID:2241958</ref> <ref>PMID:1867199</ref> <ref>PMID:1885764</ref> <ref>PMID:8161368</ref> <ref>PMID:7883996</ref> [[http://www.uniprot.org/uniprot/ODBB_HUMAN ODBB_HUMAN]] Defects in BCKDHB are the cause of maple syrup urine disease type IB (MSUD1B) [MIM:[http://omim.org/entry/248600 248600]]. MSUD is an autosomal recessive disorder characterized by mental and physical retardation, feeding problems, and a maple syrup odor to the urine.<ref>PMID:8161368</ref> <ref>PMID:11509994</ref> <ref>PMID:22326532</ref>		[[http://www.uniprot.org/uniprot/ODBA_HUMAN ODBA_HUMAN]] Defects in BCKDHA are a cause of maple syrup urine disease type IA (MSUD1A) [MIM:[http://omim.org/entry/248600 248600]]. MSUD is an autosomal recessive disorder characterized by mental and physical retardation, feeding problems, and a maple syrup odor to the urine.<ref>PMID:2060625</ref> <ref>PMID:8037208</ref> <ref>PMID:2703538</ref> <ref>PMID:2241958</ref> <ref>PMID:1867199</ref> <ref>PMID:1885764</ref> <ref>PMID:8161368</ref> <ref>PMID:7883996</ref> [[http://www.uniprot.org/uniprot/ODBB_HUMAN ODBB_HUMAN]] Defects in BCKDHB are the cause of maple syrup urine disease type IB (MSUD1B) [MIM:[http://omim.org/entry/248600 248600]]. MSUD is an autosomal recessive disorder characterized by mental and physical retardation, feeding problems, and a maple syrup odor to the urine.<ref>PMID:8161368</ref> <ref>PMID:11509994</ref> <ref>PMID:22326532</ref>
Line 35:		Line 35:
	</StructureSection>		</StructureSection>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Brautigam, C A.]]		[[Category: Brautigam, C A]]
	[[Category: Chuang, D T.]]		[[Category: Chuang, D T]]
	[[Category: Chuang, J L.]]		[[Category: Chuang, J L]]
	[[Category: Machius, M.]]		[[Category: Machius, M]]
	[[Category: Tomchick, D R.]]		[[Category: Tomchick, D R]]
	[[Category: Wynn, R M.]]		[[Category: Wynn, R M]]
	[[Category: Acylation]]		[[Category: Acylation]]
	[[Category: Maple syrup urine disease]]		[[Category: Maple syrup urine disease]]

OCA at 01:40, 30 September 2014

2014-09-30T01:40:56Z

← Older revision		Revision as of 01:40, 30 September 2014
Line 1:		Line 1:
	~~{{STRUCTURE_2bfb\| PDB=2bfb \| SCENE= }}~~		==REACTIVITY MODULATION OF HUMAN BRANCHED-CHAIN ALPHA-KETOACID DEHYDROGENASE BY AN INTERNAL MOLECULAR SWITCH==
	===REACTIVITY MODULATION OF HUMAN BRANCHED-CHAIN ALPHA-KETOACID DEHYDROGENASE BY AN INTERNAL MOLECULAR SWITCH===		<StructureSection load='2bfb' size='340' side='right' caption='[[2bfb]], [[Resolution\|resolution]] 1.77Å' scene=''>
	~~{{ABSTRACT_PUBMED_16472748}}~~		== Structural highlights ==
			<table><tr><td colspan='2'>[[2bfb]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BFB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2BFB FirstGlance]. <br>
	==Disease==		</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=MRD:(4R)-2-METHYLPENTANE-2,4-DIOL'>MRD</scene>, <scene name='pdbligand=TDP:THIAMIN+DIPHOSPHATE'>TDP</scene><br>
	[[http://www.uniprot.org/uniprot/ODBA_HUMAN ODBA_HUMAN]] Defects in BCKDHA are a cause of maple syrup urine disease type IA (MSUD1A) [MIM:[http://omim.org/entry/248600 248600]]. MSUD is an autosomal recessive disorder characterized by mental and physical retardation, feeding problems, and a maple syrup odor to the urine.<ref>PMID:2060625</ref><ref>PMID:8037208</ref><ref>PMID:2703538</ref><ref>PMID:2241958</ref><ref>PMID:1867199</ref><ref>PMID:1885764</ref><ref>PMID:8161368</ref><ref>PMID:7883996</ref> [[http://www.uniprot.org/uniprot/ODBB_HUMAN ODBB_HUMAN]] Defects in BCKDHB are the cause of maple syrup urine disease type IB (MSUD1B) [MIM:[http://omim.org/entry/248600 248600]]. MSUD is an autosomal recessive disorder characterized by mental and physical retardation, feeding problems, and a maple syrup odor to the urine.<ref>PMID:8161368</ref><ref>PMID:11509994</ref><ref>PMID:22326532</ref>		<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1dtw\|1dtw]], [[1ols\|1ols]], [[1olu\|1olu]], [[1olx\|1olx]], [[1u5b\|1u5b]], [[1v11\|1v11]], [[1v16\|1v16]], [[1v1m\|1v1m]], [[1v1r\|1v1r]], [[1wci\|1wci]], [[1x7w\|1x7w]], [[1x7x\|1x7x]], [[1x7y\|1x7y]], [[1x7z\|1x7z]], [[1x80\|1x80]], [[2beu\|2beu]], [[2bev\|2bev]], [[2bew\|2bew]], [[2bfc\|2bfc]], [[2bfd\|2bfd]], [[2bfe\|2bfe]], [[2bff\|2bff]]</td></tr>
			<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/3-methyl-2-oxobutanoate_dehydrogenase_(2-methylpropanoyl-transferring) 3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.2.4.4 1.2.4.4] </span></td></tr>
	==Function==		<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2bfb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bfb OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2bfb RCSB], [http://www.ebi.ac.uk/pdbsum/2bfb PDBsum]</span></td></tr>
			<table>
			== Disease ==
			[[http://www.uniprot.org/uniprot/ODBA_HUMAN ODBA_HUMAN]] Defects in BCKDHA are a cause of maple syrup urine disease type IA (MSUD1A) [MIM:[http://omim.org/entry/248600 248600]]. MSUD is an autosomal recessive disorder characterized by mental and physical retardation, feeding problems, and a maple syrup odor to the urine.<ref>PMID:2060625</ref> <ref>PMID:8037208</ref> <ref>PMID:2703538</ref> <ref>PMID:2241958</ref> <ref>PMID:1867199</ref> <ref>PMID:1885764</ref> <ref>PMID:8161368</ref> <ref>PMID:7883996</ref> [[http://www.uniprot.org/uniprot/ODBB_HUMAN ODBB_HUMAN]] Defects in BCKDHB are the cause of maple syrup urine disease type IB (MSUD1B) [MIM:[http://omim.org/entry/248600 248600]]. MSUD is an autosomal recessive disorder characterized by mental and physical retardation, feeding problems, and a maple syrup odor to the urine.<ref>PMID:8161368</ref> <ref>PMID:11509994</ref> <ref>PMID:22326532</ref>
			== Function ==
	[[http://www.uniprot.org/uniprot/ODBA_HUMAN ODBA_HUMAN]] The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO(2). It contains multiple copies of three enzymatic components: branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3). [[http://www.uniprot.org/uniprot/ODBB_HUMAN ODBB_HUMAN]] The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO(2). It contains multiple copies of three enzymatic components: branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3).		[[http://www.uniprot.org/uniprot/ODBA_HUMAN ODBA_HUMAN]] The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO(2). It contains multiple copies of three enzymatic components: branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3). [[http://www.uniprot.org/uniprot/ODBB_HUMAN ODBB_HUMAN]] The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO(2). It contains multiple copies of three enzymatic components: branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3).
			== Evolutionary Conservation ==
			[[Image:Consurf_key_small.gif\|200px\|right]]
			Check<jmol>
			<jmolCheckbox>
			<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bf/2bfb_consurf.spt"</scriptWhenChecked>
			<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
			<text>to colour the structure by Evolutionary Conservation</text>
			</jmolCheckbox>
			</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
			<div style="clear:both"></div>
			<div style="background-color:#fffaf0;">
			== Publication Abstract from PubMed ==
			The dehydrogenase/decarboxylase (E1b) component of the 4 MD human branched-chain alpha-ketoacid dehydrogenase complex (BCKDC) is a thiamin diphosphate (ThDP)-dependent enzyme. We have determined the crystal structures of E1b with ThDP bound intermediates after decarboxylation of alpha-ketoacids. We show that a key tyrosine residue in the E1b active site functions as a conformational switch to reduce the reactivity of the ThDP cofactor through interactions with its thiazolium ring. The intermediates do not assume the often-postulated enamine state, but likely a carbanion state. The carbanion presumably facilitates the second E1b-catalyzed reaction, involving the transfer of an acyl moiety from the intermediate to a lipoic acid prosthetic group in the transacylase (E2b) component of the BCKDC. The tyrosine switch further remodels an E1b loop region to promote E1b binding to E2b. Our results illustrate the versatility of the tyrosine switch in coordinating the catalytic events in E1b by modulating the reactivity of reaction intermediates.

	~~==About this~~ Structure==		A versatile conformational switch regulates reactivity in human branched-chain alpha-ketoacid dehydrogenase.,Machius M, Wynn RM, Chuang JL, Li J, Kluger R, Yu D, Tomchick DR, Brautigam CA, Chuang DT Structure. 2006 Feb;14(2):287-98. PMID:16472748<ref>PMID:16472748</ref>
	~~[[2bfb]] is a~~ 2 ~~chain structure with sequence from [http~~:~~//en~~.~~wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http~~:/~~/oca.weizmann.ac.il/oca-bin/ocashort?id=2BFB OCA].~~

	~~==Reference==~~		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	<~~ref group="xtra"~~>~~PMID:016472748~~</~~ref~~>~~<ref group~~=~~"xtra">PMID:015166214</ref><ref group~~=~~"xtra">PMID:012902323</ref><ref group~~=~~"xtra">PMID:011069910</ref>~~<references ~~group="xtra"~~/><~~references~~/>		</div>
			== References ==
			<references/>
			__TOC__
			</StructureSection>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Brautigam, C A.]]		[[Category: Brautigam, C A.]]

OCA at 12:17, 24 March 2013

2013-03-24T12:17:33Z

← Older revision		Revision as of 12:17, 24 March 2013
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	~~[[Image:2bfb.png\|left\|200px]]~~

	~~<!--~~
	~~The line below this paragraph, containing "STRUCTURE_2bfb", creates the "Structure Box" on the page.~~
	~~You may change the PDB parameter (which sets the PDB file loaded into the applet)~~
	~~or the SCENE parameter (which sets the initial scene displayed when the page is loaded),~~
	~~or leave the SCENE parameter empty for the default display.~~
	~~-->~~
	{{STRUCTURE_2bfb\| PDB=2bfb \| SCENE= }}		{{STRUCTURE_2bfb\| PDB=2bfb \| SCENE= }}

	===REACTIVITY MODULATION OF HUMAN BRANCHED-CHAIN ALPHA-KETOACID DEHYDROGENASE BY AN INTERNAL MOLECULAR SWITCH===		===REACTIVITY MODULATION OF HUMAN BRANCHED-CHAIN ALPHA-KETOACID DEHYDROGENASE BY AN INTERNAL MOLECULAR SWITCH===
			{{ABSTRACT_PUBMED_16472748}}

			==Disease==
			[[http://www.uniprot.org/uniprot/ODBA_HUMAN ODBA_HUMAN]] Defects in BCKDHA are a cause of maple syrup urine disease type IA (MSUD1A) [MIM:[http://omim.org/entry/248600 248600]]. MSUD is an autosomal recessive disorder characterized by mental and physical retardation, feeding problems, and a maple syrup odor to the urine.<ref>PMID:2060625</ref><ref>PMID:8037208</ref><ref>PMID:2703538</ref><ref>PMID:2241958</ref><ref>PMID:1867199</ref><ref>PMID:1885764</ref><ref>PMID:8161368</ref><ref>PMID:7883996</ref> [[http://www.uniprot.org/uniprot/ODBB_HUMAN ODBB_HUMAN]] Defects in BCKDHB are the cause of maple syrup urine disease type IB (MSUD1B) [MIM:[http://omim.org/entry/248600 248600]]. MSUD is an autosomal recessive disorder characterized by mental and physical retardation, feeding problems, and a maple syrup odor to the urine.<ref>PMID:8161368</ref><ref>PMID:11509994</ref><ref>PMID:22326532</ref>

	<!--		==Function==
	~~The line below this paragraph, {{ABSTRACT_PUBMED_16472748}}, adds~~ the ~~Publication Abstract~~ to ~~the page~~		[[http://www.uniprot.org/uniprot/ODBA_HUMAN ODBA_HUMAN]] The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO(2). It contains multiple copies of three enzymatic components: branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3). [[http://www.uniprot.org/uniprot/ODBB_HUMAN ODBB_HUMAN]] The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO(2). It contains multiple copies of three enzymatic components: branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3).
	(~~as it appears on PubMed at~~ http://www.~~pubmed~~.~~gov~~)~~, where 16472748 is the PubMed ID number~~.
	-->
	~~{{ABSTRACT_PUBMED_16472748}}~~

	==About this Structure==		==About this Structure==
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	==Reference==		==Reference==
	<ref group="xtra">PMID:016472748</ref><ref group="xtra">PMID:015166214</ref><ref group="xtra">PMID:012902323</ref><ref group="xtra">PMID:011069910</ref><references group="xtra"/>		<ref group="xtra">PMID:016472748</ref><ref group="xtra">PMID:015166214</ref><ref group="xtra">PMID:012902323</ref><ref group="xtra">PMID:011069910</ref><references group="xtra"/><references/>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Brautigam, C A.]]		[[Category: Brautigam, C A.]]

← Older revision		Revision as of 10:31, 17 February 2021
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	<StructureSection load='2bfb' size='340' side='right'caption='[[2bfb]], [[Resolution\|resolution]] 1.77Å' scene=''>		<StructureSection load='2bfb' size='340' side='right'caption='[[2bfb]], [[Resolution\|resolution]] 1.77Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2bfb]] is a 2 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BFB OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=2BFB FirstGlance]. <br>		<table><tr><td colspan='2'>[[2bfb]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BFB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BFB FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=MRD:(4R)-2-METHYLPENTANE-2,4-DIOL'>MRD</scene>, <scene name='pdbligand=TDP:THIAMIN+DIPHOSPHATE'>TDP</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=MRD:(4R)-2-METHYLPENTANE-2,4-DIOL'>MRD</scene>, <scene name='pdbligand=TDP:THIAMIN+DIPHOSPHATE'>TDP</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1dtw\|1dtw]], [[1ols\|1ols]], [[1olu\|1olu]], [[1olx\|1olx]], [[1u5b\|1u5b]], [[1v11\|1v11]], [[1v16\|1v16]], [[1v1m\|1v1m]], [[1v1r\|1v1r]], [[1wci\|1wci]], [[1x7w\|1x7w]], [[1x7x\|1x7x]], [[1x7y\|1x7y]], [[1x7z\|1x7z]], [[1x80\|1x80]], [[2beu\|2beu]], [[2bev\|2bev]], [[2bew\|2bew]], [[2bfc\|2bfc]], [[2bfd\|2bfd]], [[2bfe\|2bfe]], [[2bff\|2bff]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1dtw\|1dtw]], [[1ols\|1ols]], [[1olu\|1olu]], [[1olx\|1olx]], [[1u5b\|1u5b]], [[1v11\|1v11]], [[1v16\|1v16]], [[1v1m\|1v1m]], [[1v1r\|1v1r]], [[1wci\|1wci]], [[1x7w\|1x7w]], [[1x7x\|1x7x]], [[1x7y\|1x7y]], [[1x7z\|1x7z]], [[1x80\|1x80]], [[2beu\|2beu]], [[2bev\|2bev]], [[2bew\|2bew]], [[2bfc\|2bfc]], [[2bfd\|2bfd]], [[2bfe\|2bfe]], [[2bff\|2bff]]</div></td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://en.wikipedia.org/wiki/3-methyl-2-oxobutanoate_dehydrogenase_(2-methylpropanoyl-transferring) 3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring)], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.2.4.4 1.2.4.4] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/3-methyl-2-oxobutanoate_dehydrogenase_(2-methylpropanoyl-transferring) 3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring)], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.2.4.4 1.2.4.4] </span></td></tr>
	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=2bfb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bfb OCA], [~~http~~://pdbe.org/2bfb PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=2bfb RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/2bfb PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=2bfb ProSAT]</span></td></tr>		<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2bfb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bfb OCA], [https://pdbe.org/2bfb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2bfb RCSB], [https://www.ebi.ac.uk/pdbsum/2bfb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2bfb ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
	[[~~http~~://www.uniprot.org/uniprot/ODBA_HUMAN ODBA_HUMAN]] Defects in BCKDHA are a cause of maple syrup urine disease type IA (MSUD1A) [MIM:[~~http~~://omim.org/entry/248600 248600]]. MSUD is an autosomal recessive disorder characterized by mental and physical retardation, feeding problems, and a maple syrup odor to the urine.<ref>PMID:2060625</ref> <ref>PMID:8037208</ref> <ref>PMID:2703538</ref> <ref>PMID:2241958</ref> <ref>PMID:1867199</ref> <ref>PMID:1885764</ref> <ref>PMID:8161368</ref> <ref>PMID:7883996</ref> [[~~http~~://www.uniprot.org/uniprot/ODBB_HUMAN ODBB_HUMAN]] Defects in BCKDHB are the cause of maple syrup urine disease type IB (MSUD1B) [MIM:[~~http~~://omim.org/entry/248600 248600]]. MSUD is an autosomal recessive disorder characterized by mental and physical retardation, feeding problems, and a maple syrup odor to the urine.<ref>PMID:8161368</ref> <ref>PMID:11509994</ref> <ref>PMID:22326532</ref>		[[https://www.uniprot.org/uniprot/ODBA_HUMAN ODBA_HUMAN]] Defects in BCKDHA are a cause of maple syrup urine disease type IA (MSUD1A) [MIM:[https://omim.org/entry/248600 248600]]. MSUD is an autosomal recessive disorder characterized by mental and physical retardation, feeding problems, and a maple syrup odor to the urine.<ref>PMID:2060625</ref> <ref>PMID:8037208</ref> <ref>PMID:2703538</ref> <ref>PMID:2241958</ref> <ref>PMID:1867199</ref> <ref>PMID:1885764</ref> <ref>PMID:8161368</ref> <ref>PMID:7883996</ref> [[https://www.uniprot.org/uniprot/ODBB_HUMAN ODBB_HUMAN]] Defects in BCKDHB are the cause of maple syrup urine disease type IB (MSUD1B) [MIM:[https://omim.org/entry/248600 248600]]. MSUD is an autosomal recessive disorder characterized by mental and physical retardation, feeding problems, and a maple syrup odor to the urine.<ref>PMID:8161368</ref> <ref>PMID:11509994</ref> <ref>PMID:22326532</ref>
	== Function ==		== Function ==
	[[~~http~~://www.uniprot.org/uniprot/ODBA_HUMAN ODBA_HUMAN]] The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO(2). It contains multiple copies of three enzymatic components: branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3). [[~~http~~://www.uniprot.org/uniprot/ODBB_HUMAN ODBB_HUMAN]] The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO(2). It contains multiple copies of three enzymatic components: branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3).		[[https://www.uniprot.org/uniprot/ODBA_HUMAN ODBA_HUMAN]] The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO(2). It contains multiple copies of three enzymatic components: branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3). [[https://www.uniprot.org/uniprot/ODBB_HUMAN ODBB_HUMAN]] The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO(2). It contains multiple copies of three enzymatic components: branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3).
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]