2bdo - Revision history

OCA at 05:06, 17 October 2024

2024-10-17T05:06:52Z

← Older revision		Revision as of 05:06, 17 October 2024
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	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2bdo]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_BL21(DE3) Escherichia coli BL21(DE3)]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BDO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BDO FirstGlance]. <br>		<table><tr><td colspan='2'>[[2bdo]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_BL21(DE3) Escherichia coli BL21(DE3)]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BDO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BDO FirstGlance]. <br>
	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>		</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 23 models</td></tr>
	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BTN:BIOTIN'>BTN</scene></td></tr>		<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BTN:BIOTIN'>BTN</scene></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=2bdo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bdo OCA], [https://pdbe.org/2bdo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2bdo RCSB], [https://www.ebi.ac.uk/pdbsum/2bdo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2bdo 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=2bdo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bdo OCA], [https://pdbe.org/2bdo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2bdo RCSB], [https://www.ebi.ac.uk/pdbsum/2bdo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2bdo ProSAT]</span></td></tr>
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	<jmolCheckbox>		<jmolCheckbox>
	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bd/2bdo_consurf.spt"</scriptWhenChecked>		<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bd/2bdo_consurf.spt"</scriptWhenChecked>
	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/~~initialview01~~.spt</scriptWhenUnchecked>		<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
	</jmolCheckbox>		</jmolCheckbox>

OCA at 00:07, 28 December 2023

2023-12-28T00:07:05Z

← Older revision		Revision as of 00:07, 28 December 2023
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	==SOLUTION STRUCTURE OF HOLO-BIOTINYL DOMAIN FROM ACETYL COENZYME A CARBOXYLASE OF ESCHERICHIA COLI DETERMINED BY TRIPLE-RESONANCE NMR SPECTROSCOPY==		==SOLUTION STRUCTURE OF HOLO-BIOTINYL DOMAIN FROM ACETYL COENZYME A CARBOXYLASE OF ESCHERICHIA COLI DETERMINED BY TRIPLE-RESONANCE NMR SPECTROSCOPY==
	<StructureSection load='2bdo' size='340' side='right'caption='[[2bdo~~]], [[NMR_Ensembles_of_Models \| 23 NMR models~~]]' scene=''>		<StructureSection load='2bdo' size='340' side='right'caption='[[2bdo]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2bdo]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Ecobd Ecobd~~]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BDO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BDO FirstGlance]. <br>		<table><tr><td colspan='2'>[[2bdo]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_BL21(DE3) Escherichia coli BL21(DE3)]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BDO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BDO FirstGlance]. <br>
	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=BTN:BIOTIN'>BTN</scene>~~</td></tr>		</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
	<tr id='~~activity~~'><td class="sblockLbl"><b>~~Activity~~:</b></td><td class="sblockDat"><~~span class~~='~~plainlinks~~'>~~[https://en.wikipedia.org/wiki/Acetyl-CoA_carboxylase Acetyl-CoA carboxylase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.4.1.2 6.4.1.2]~~ </~~span~~></td></tr>		<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BTN:BIOTIN'>BTN</scene></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=2bdo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bdo OCA], [https://pdbe.org/2bdo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2bdo RCSB], [https://www.ebi.ac.uk/pdbsum/2bdo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2bdo 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=2bdo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bdo OCA], [https://pdbe.org/2bdo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2bdo RCSB], [https://www.ebi.ac.uk/pdbsum/2bdo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2bdo ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[[https://www.uniprot.org/uniprot/BCCP_ECOLI BCCP_ECOLI]] This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA.		[https://www.uniprot.org/uniprot/BCCP_ECOLI BCCP_ECOLI] This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA.
	== 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: Acetyl-CoA carboxylase]]~~
	~~[[Category: Ecobd]]~~
	[[Category: Large Structures]]		[[Category: Large Structures]]
	[[Category: Broadhurst~~, R W~~]]		[[Category: Broadhurst RW]]
	[[Category: Chapman-Smith, A]]		[[Category: Chapman-Smith A]]
	[[Category: Cronan~~, J E~~]]		[[Category: Cronan JE]]
	[[Category: Howard~~, M J~~]]		[[Category: Howard MJ]]
	[[Category: Morris, T]]		[[Category: Morris T]]
	[[Category: Perham~~, R N~~]]		[[Category: Perham RN]]
	[[Category: Roberts~~, E L~~]]		[[Category: Roberts EL]]
	[[Category: Shu, N]]		[[Category: Shu N]]
	[[Category: Wallace~~, J C]]~~		[[Category: Wallace JC]]
	~~[[Category: Acetyl coa carboxylase]]~~
	~~[[Category: Biotin]]~~
	~~[[Category: Biotinyl domain]]~~
	~~[[Category: Nmr spectroscopy]]~~
	~~[[Category: Protein structure]]~~
	~~[[Category: Swinging arm~~]]

OCA at 13:08, 24 November 2021

2021-11-24T13:08:18Z

← Older revision		Revision as of 13:08, 24 November 2021
Line 3:		Line 3:
	<StructureSection load='2bdo' size='340' side='right'caption='[[2bdo]], [[NMR_Ensembles_of_Models \| 23 NMR models]]' scene=''>		<StructureSection load='2bdo' size='340' side='right'caption='[[2bdo]], [[NMR_Ensembles_of_Models \| 23 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2bdo]] is a 1 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Ecobd Ecobd]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BDO OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=2BDO FirstGlance]. <br>		<table><tr><td colspan='2'>[[2bdo]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Ecobd Ecobd]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BDO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BDO FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BTN:BIOTIN'>BTN</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BTN:BIOTIN'>BTN</scene></td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://en.wikipedia.org/wiki/Acetyl-CoA_carboxylase Acetyl-CoA carboxylase], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.4.1.2 6.4.1.2] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Acetyl-CoA_carboxylase Acetyl-CoA carboxylase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.4.1.2 6.4.1.2] </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=2bdo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bdo OCA], [~~http~~://pdbe.org/2bdo PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=2bdo RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/2bdo PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=2bdo 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=2bdo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bdo OCA], [https://pdbe.org/2bdo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2bdo RCSB], [https://www.ebi.ac.uk/pdbsum/2bdo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2bdo ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[[~~http~~://www.uniprot.org/uniprot/BCCP_ECOLI BCCP_ECOLI]] This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA.		[[https://www.uniprot.org/uniprot/BCCP_ECOLI BCCP_ECOLI]] This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]

OCA at 08:04, 19 February 2020

2020-02-19T08:04:52Z

← Older revision		Revision as of 08:04, 19 February 2020
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	==SOLUTION STRUCTURE OF HOLO-BIOTINYL DOMAIN FROM ACETYL COENZYME A CARBOXYLASE OF ESCHERICHIA COLI DETERMINED BY TRIPLE-RESONANCE NMR SPECTROSCOPY==		==SOLUTION STRUCTURE OF HOLO-BIOTINYL DOMAIN FROM ACETYL COENZYME A CARBOXYLASE OF ESCHERICHIA COLI DETERMINED BY TRIPLE-RESONANCE NMR SPECTROSCOPY==
	<StructureSection load='2bdo' size='340' side='right' caption='[[2bdo]], [[NMR_Ensembles_of_Models \| 23 NMR models]]' scene=''>		<StructureSection load='2bdo' size='340' side='right'caption='[[2bdo]], [[NMR_Ensembles_of_Models \| 23 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2bdo]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecobd Ecobd]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BDO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2BDO FirstGlance]. <br>		<table><tr><td colspan='2'>[[2bdo]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecobd Ecobd]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BDO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2BDO FirstGlance]. <br>
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	==See Also==		==See Also==
	*[[Acetyl-CoA carboxylase\|Acetyl-CoA carboxylase]]		*[[Acetyl-CoA carboxylase 3D structures\|Acetyl-CoA carboxylase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
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	[[Category: Acetyl-CoA carboxylase]]		[[Category: Acetyl-CoA carboxylase]]
	[[Category: Ecobd]]		[[Category: Ecobd]]
			[[Category: Large Structures]]
	[[Category: Broadhurst, R W]]		[[Category: Broadhurst, R W]]
	[[Category: Chapman-Smith, A]]		[[Category: Chapman-Smith, A]]

OCA at 06:28, 16 May 2018

2018-05-16T06:28:52Z

← Older revision		Revision as of 06:28, 16 May 2018
Line 1:		Line 1:

	==SOLUTION STRUCTURE OF HOLO-BIOTINYL DOMAIN FROM ACETYL COENZYME A CARBOXYLASE OF ESCHERICHIA COLI DETERMINED BY TRIPLE-RESONANCE NMR SPECTROSCOPY==		==SOLUTION STRUCTURE OF HOLO-BIOTINYL DOMAIN FROM ACETYL COENZYME A CARBOXYLASE OF ESCHERICHIA COLI DETERMINED BY TRIPLE-RESONANCE NMR SPECTROSCOPY==
	<StructureSection load='2bdo' size='340' side='right' caption='[[2bdo]], [[NMR_Ensembles_of_Models \| 23 NMR models]]' scene=''>		<StructureSection load='2bdo' size='340' side='right' caption='[[2bdo]], [[NMR_Ensembles_of_Models \| 23 NMR models]]' scene=''>
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	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BTN:BIOTIN'>BTN</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BTN:BIOTIN'>BTN</scene></td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Acetyl-CoA_carboxylase Acetyl-CoA carboxylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.4.1.2 6.4.1.2] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Acetyl-CoA_carboxylase Acetyl-CoA carboxylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.4.1.2 6.4.1.2] </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=2bdo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bdo OCA], [http://pdbe.org/2bdo PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2bdo RCSB], [http://www.ebi.ac.uk/pdbsum/2bdo 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=2bdo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bdo OCA], [http://pdbe.org/2bdo PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2bdo RCSB], [http://www.ebi.ac.uk/pdbsum/2bdo PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2bdo ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 13:		Line 14:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bd/2bdo_consurf.spt"</scriptWhenChecked>		<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bd/2bdo_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=2bdo ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">

OCA at 07:44, 11 September 2015

2015-09-11T07:44:36Z

← Older revision		Revision as of 07:44, 11 September 2015
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	<StructureSection load='2bdo' size='340' side='right' caption='[[2bdo]], [[NMR_Ensembles_of_Models \| 23 NMR models]]' scene=''>		<StructureSection load='2bdo' size='340' side='right' caption='[[2bdo]], [[NMR_Ensembles_of_Models \| 23 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2bdo]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Escherichia_coli_bl21(de3) Escherichia coli bl21(de3)~~]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BDO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2BDO FirstGlance]. <br>		<table><tr><td colspan='2'>[[2bdo]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecobd Ecobd]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BDO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2BDO FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BTN:BIOTIN'>BTN</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BTN:BIOTIN'>BTN</scene></td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Acetyl-CoA_carboxylase Acetyl-CoA carboxylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.4.1.2 6.4.1.2] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Acetyl-CoA_carboxylase Acetyl-CoA carboxylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.4.1.2 6.4.1.2] </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=2bdo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bdo OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2bdo RCSB], [http://www.ebi.ac.uk/pdbsum/2bdo 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=2bdo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bdo OCA], [http://pdbe.org/2bdo PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2bdo RCSB], [http://www.ebi.ac.uk/pdbsum/2bdo PDBsum]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
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	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 2bdo" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
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	</StructureSection>		</StructureSection>
	[[Category: Acetyl-CoA carboxylase]]		[[Category: Acetyl-CoA carboxylase]]
			[[Category: Ecobd]]
	[[Category: Broadhurst, R W]]		[[Category: Broadhurst, R W]]
	[[Category: Chapman-Smith, A]]		[[Category: Chapman-Smith, A]]

OCA at 13:24, 25 December 2014

2014-12-25T13:24:35Z

← Older revision		Revision as of 13:24, 25 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2bdo]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli_bl21(de3) Escherichia coli bl21(de3)]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BDO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2BDO FirstGlance]. <br>		<table><tr><td colspan='2'>[[2bdo]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli_bl21(de3) Escherichia coli bl21(de3)]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BDO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2BDO FirstGlance]. <br>
	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BTN:BIOTIN'>BTN</scene><br>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BTN:BIOTIN'>BTN</scene></td></tr>
	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Acetyl-CoA_carboxylase Acetyl-CoA carboxylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.4.1.2 6.4.1.2] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Acetyl-CoA_carboxylase Acetyl-CoA carboxylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.4.1.2 6.4.1.2] </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=2bdo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bdo OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2bdo RCSB], [http://www.ebi.ac.uk/pdbsum/2bdo 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=2bdo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bdo OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2bdo RCSB], [http://www.ebi.ac.uk/pdbsum/2bdo PDBsum]</span></td></tr>
	<table>		</table>
			== Function ==
			[[http://www.uniprot.org/uniprot/BCCP_ECOLI BCCP_ECOLI]] This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
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	</StructureSection>		</StructureSection>
	[[Category: Acetyl-CoA carboxylase]]		[[Category: Acetyl-CoA carboxylase]]
	[[Category: Broadhurst, R W.]]		[[Category: Broadhurst, R W]]
	[[Category: Chapman-Smith, A.]]		[[Category: Chapman-Smith, A]]
	[[Category: Cronan, J E.]]		[[Category: Cronan, J E]]
	[[Category: Howard, M J.]]		[[Category: Howard, M J]]
	[[Category: Morris, T.]]		[[Category: Morris, T]]
	[[Category: Perham, R N.]]		[[Category: Perham, R N]]
	[[Category: Roberts, E L.]]		[[Category: Roberts, E L]]
	[[Category: Shu, N.]]		[[Category: Shu, N]]
	[[Category: Wallace, J C.]]		[[Category: Wallace, J C]]
	[[Category: Acetyl coa carboxylase]]		[[Category: Acetyl coa carboxylase]]
	[[Category: Biotin]]		[[Category: Biotin]]

OCA at 04:37, 29 September 2014

2014-09-29T04:37:24Z

← Older revision		Revision as of 04:37, 29 September 2014
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	[[Image:~~2bdo~~.~~png~~\|~~left~~\|~~200px~~]]		==SOLUTION STRUCTURE OF HOLO-BIOTINYL DOMAIN FROM ACETYL COENZYME A CARBOXYLASE OF ESCHERICHIA COLI DETERMINED BY TRIPLE-RESONANCE NMR SPECTROSCOPY==
			<StructureSection load='2bdo' size='340' side='right' caption='[[2bdo]], [[NMR_Ensembles_of_Models \| 23 NMR models]]' scene=''>
			== Structural highlights ==
			<table><tr><td colspan='2'>[[2bdo]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli_bl21(de3) Escherichia coli bl21(de3)]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BDO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2BDO FirstGlance]. <br>
			</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BTN:BIOTIN'>BTN</scene><br>
			<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Acetyl-CoA_carboxylase Acetyl-CoA carboxylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.4.1.2 6.4.1.2] </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=2bdo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bdo OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2bdo RCSB], [http://www.ebi.ac.uk/pdbsum/2bdo PDBsum]</span></td></tr>
			<table>
			== 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/bd/2bdo_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 ==
			A subgene encoding the 87 C-terminal amino acids of the biotinyl carboxy carrier protein (BCCP) from the acetyl CoA carboxylase of Escherichia coli was overexpressed and the apoprotein biotinylated in vitro. The structures of both the apo and holo forms of the biotinyl domain were determined by means of multidimensional NMR spectroscopy. That of the holo domain was well-defined, except for the 10 N-terminal residues, which form part of the flexible linker between the biotinyl and subunit-binding domains of BCCP. In agreement with X-ray crystallographic studies [Athappilly, F. K., and Hendrickson, W. A. (1995) Structure 3, 1407-1419], the structure comprises a flattened beta-barrel composed of two four-stranded beta-sheets with a 2-fold axis of quasi-symmetry and the biotinyl-lysine residue displayed in an exposed beta-turn on the side of the protein opposite from the N- and C-terminal residues. The biotin group is immobilized on the protein surface, with the ureido ring held down by interactions with a protruding polypeptide "thumb" formed by residues 94-101. However, at the site of carboxylation, no evidence could be found in solution for the predicted hydrogen bond between the main chain O of Thr94 and the ureido HN1'. The structure of the apo domain is essentially identical, although the packing of side chains is more favorable in the holo domain, and this may be reflected in differences in the dynamics of the two forms. The thumb region appears to be lacking in almost all other biotinyl domain sequences, and it may be that the immobilization of the biotinyl-lysine residue in the biotinyl domain of BCCP is an unusual requirement, needed for the catalytic reaction of acetyl CoA carboxylase.

	~~{{STRUCTURE_2bdo\| PDB=2bdo \| SCENE= }}~~		Solution structures of apo and holo biotinyl domains from acetyl coenzyme A carboxylase of Escherichia coli determined by triple-resonance nuclear magnetic resonance spectroscopy.,Roberts EL, Shu N, Howard MJ, Broadhurst RW, Chapman-Smith A, Wallace JC, Morris T, Cronan JE Jr, Perham RN Biochemistry. 1999 Apr 20;38(16):5045-53. PMID:10213607<ref>PMID:10213607</ref>

	~~===SOLUTION STRUCTURE OF HOLO-BIOTINYL DOMAIN FROM ACETYL COENZYME A CARBOXYLASE OF ESCHERICHIA COLI DETERMINED BY TRIPLE-RESONANCE NMR SPECTROSCOPY===~~		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
			</div>
	~~{{ABSTRACT_PUBMED_10213607}}~~

	~~==About this Structure==~~
	~~[[2bdo]] is~~ a ~~1 chain structure with sequence from [http://en.wikipedia~~.~~org/wiki/Escherichia_coli_bl21(de3) Escherichia coli bl21(de3)]~~. ~~Full experimental information is available from [http://oca~~.~~weizmann.ac.il/oca-bin~~/~~ocashort?id=2BDO OCA].~~

	==See Also==		==See Also==
	*[[Acetyl-CoA carboxylase\|Acetyl-CoA carboxylase]]		*[[Acetyl-CoA carboxylase\|Acetyl-CoA carboxylase]]
			== References ==
	==~~Reference~~==		<references/>
	<~~ref group="xtra">PMID:010213607<~~/~~ref~~><~~references group="xtra"~~/>		__TOC__
			</StructureSection>
	[[Category: Acetyl-CoA carboxylase]]		[[Category: Acetyl-CoA carboxylase]]
	[[Category: Broadhurst, R W.]]		[[Category: Broadhurst, R W.]]

OCA at 17:12, 20 October 2012

2012-10-20T17:12:22Z

← Older revision		Revision as of 17:12, 20 October 2012
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	==About this Structure==		==About this Structure==
	[[2bdo]] is a 1 chain structure ~~of [[Acetyl-CoA carboxylase]]~~ with sequence from [http://en.wikipedia.org/wiki/~~Escherichia_coli~~ Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BDO OCA].		[[2bdo]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli_bl21(de3) Escherichia coli bl21(de3)]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BDO OCA].

	==See Also==		==See Also==
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	<ref group="xtra">PMID:010213607</ref><references group="xtra"/>		<ref group="xtra">PMID:010213607</ref><references group="xtra"/>
	[[Category: Acetyl-CoA carboxylase]]		[[Category: Acetyl-CoA carboxylase]]
	~~[[Category: Escherichia coli]]~~
	[[Category: Broadhurst, R W.]]		[[Category: Broadhurst, R W.]]
	[[Category: Chapman-Smith, A.]]		[[Category: Chapman-Smith, A.]]

OCA: Protected "2bdo" [edit=sysop:move=sysop]

2012-07-27T00:10:25Z

Protected "2bdo" [edit=sysop:move=sysop]

← Older revision	Revision as of 00:10, 27 July 2012
(No difference)