2ed4 - Revision history

OCA at 06:25, 3 April 2024

2024-04-03T06:25:19Z

← Older revision		Revision as of 06:25, 3 April 2024
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	<StructureSection load='2ed4' size='340' side='right'caption='[[2ed4]], [[Resolution\|resolution]] 1.85Å' scene=''>		<StructureSection load='2ed4' size='340' side='right'caption='[[2ed4]], [[Resolution\|resolution]] 1.85Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2ed4]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Thet8 Thet8~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ED4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ED4 FirstGlance]. <br>		<table><tr><td colspan='2'>[[2ed4]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_thermophilus_HB8 Thermus thermophilus HB8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ED4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ED4 FirstGlance]. <br>
	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=FAD:FLAVIN~~-~~ADENINE+DINUCLEOTIDE'>FAD</scene>~~, ~~<scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</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]] 1.85Å</td></tr>
	<tr id='~~related~~'><td class="sblockLbl"><b>[[~~Related_structure~~\|~~Related~~:]]</b></td><td class="sblockDat"><~~div style~~='~~overflow~~: ~~auto; max~~-~~height: 3em;~~'>~~[[2ecr\|2ecr]], [[2ecu\|2ecu]]~~</~~div~~><~~/td></tr>~~		<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene></td></tr>
	~~<tr id~~='~~gene'><td class~~=~~"sblockLbl"><b>[[Gene\|Gene~~:~~]]</b~~></~~td><td class="sblockDat"~~>~~TTHA0961 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=300852 THET8])~~</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=2ed4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ed4 OCA], [https://pdbe.org/2ed4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ed4 RCSB], [https://www.ebi.ac.uk/pdbsum/2ed4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ed4 ProSAT], [https://www.topsan.org/Proteins/RSGI/2ed4 TOPSAN]</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=2ed4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ed4 OCA], [https://pdbe.org/2ed4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ed4 RCSB], [https://www.ebi.ac.uk/pdbsum/2ed4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ed4 ProSAT], [https://www.topsan.org/Proteins/RSGI/2ed4 TOPSAN]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[[https://www.uniprot.org/uniprot/HPAC_THET8 HPAC_THET8]] Catalyzes the reduction of free flavins (FMN, FAD and riboflavin) by NADH. Subsequently, the reduced flavins diffuse to the large HpaB component.<ref>PMID:17729270</ref>		[https://www.uniprot.org/uniprot/HPAC_THET8 HPAC_THET8] Catalyzes the reduction of free flavins (FMN, FAD and riboflavin) by NADH. Subsequently, the reduced flavins diffuse to the large HpaB component.<ref>PMID:17729270</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
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	</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=2ed4 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=2ed4 ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	~~<div style="background-color:#fffaf0;">~~
	~~== Publication Abstract from PubMed ==~~
	The two-component enzyme, 4-hydroxyphenylacetate 3-monooxygenase, catalyzes the conversion of 4-hydroxyphenylacetate to 3,4-dihydroxyphenylacetate. In the overall reaction, the oxygenase component (HpaB) introduces a hydroxyl group into the benzene ring of 4-hydroxyphenylacetate using molecular oxygen and reduced flavin, while the reductase component (HpaC) provides free reduced flavins for HpaB. The crystal structures of HpaC from Thermus thermophilus HB8 in the ligand-free form, the FAD-containing form, and the ternary complex with FAD and NAD(+) were determined. In the ligand-free form, two large grooves are present at the dimer interface, and are occupied by water molecules. A structural analysis of HpaC containing FAD revealed that FAD has a low occupancy, indicating that it is not tightly bound to HpaC. This was further confirmed in flavin dissociation experiments, showing that FAD can be released from HpaC. The structure of the ternary complex revealed that FAD and NAD(+) are bound in the groove in the extended and folded conformation, respectively. The nicotinamide ring of NAD(+) is sandwiched between the adenine ring of NAD(+) and the isoalloxazine ring of FAD. The distance between N5 of the isoalloxazine ring and C4 of the nicotinamide ring is about 3.3 A, sufficient to permit hydride transfer. The structures of these three states are essentially identical, however, the side chains of several residues show small conformational changes, indicating an induced fit upon binding of NADH. Inactivity with respect to NADPH can be explained as instability of the binding of NADPH with the negatively charged 2'-phosphate group buried inside the complex, as well as a possible repulsive effect by the dipole of helix alpha1. A comparison of the binding mode of FAD with that in PheA2 from Bacillus thermoglucosidasius A7, which contains FAD as a prosthetic group, reveals remarkable conformational differences in a less conserved loop region (Gly83-Gly94) involved in the binding of the AMP moiety of FAD. These data suggest that variations in the affinities for FAD in the reductases of the two-component flavin-diffusible monooxygenase family may be attributed to difference in the interaction between the AMP moiety of FAD and the less conserved loop region which possibly shows structural divergence.

	Crystal structure of the flavin reductase component (HpaC) of 4-hydroxyphenylacetate 3-monooxygenase from Thermus thermophilus HB8: Structural basis for the flavin affinity.,Kim SH, Hisano T, Iwasaki W, Ebihara A, Miki K Proteins. 2008 Feb 15;70(3):718-30. PMID:17729270<ref>PMID:17729270</ref>

	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~
	~~</div>~~
	~~<div class="pdbe-citations 2ed4" style="background-color:#fffaf0;"></div>~~
	== References ==		== References ==
	<references/>		<references/>
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	</StructureSection>		</StructureSection>
	[[Category: Large Structures]]		[[Category: Large Structures]]
	[[Category: ~~Thet8~~]]		[[Category: Thermus thermophilus HB8]]
	[[Category: Ebihara, A]]		[[Category: Ebihara A]]
	[[Category: Hisano, T]]		[[Category: Hisano T]]
	[[Category: Iwasaki, W]]		[[Category: Iwasaki W]]
	[[Category: Kim~~, S H~~]]		[[Category: Kim SH]]
	[[Category: Miki, K]]		[[Category: Miki K]]
	~~[[Category: Flavin diffusible]]~~
	~~[[Category: Flavin reductase]]~~
	~~[[Category: Oxidoreductase]]~~
	~~[[Category: Two-component monooxygenase~~]]

OCA at 11:59, 10 February 2021

2021-02-10T11:59:54Z

← Older revision		Revision as of 11:59, 10 February 2021
Line 1:		Line 1:

	==Crystal structure of flavin reductase HpaC complexed with FAD and NAD==		==Crystal structure of flavin reductase HpaC complexed with FAD and NAD==
	<StructureSection load='2ed4' size='340' side='right' caption='[[2ed4]], [[Resolution\|resolution]] 1.85Å' scene=''>		<StructureSection load='2ed4' size='340' side='right'caption='[[2ed4]], [[Resolution\|resolution]] 1.85Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2ed4]] is a 2 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Thet8 Thet8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ED4 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=2ED4 FirstGlance]. <br>		<table><tr><td colspan='2'>[[2ed4]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Thet8 Thet8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ED4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ED4 FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2ecr\|2ecr]], [[2ecu\|2ecu]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2ecr\|2ecr]], [[2ecu\|2ecu]]</div></td></tr>
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">TTHA0961 ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=300852 THET8])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">TTHA0961 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=300852 THET8])</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=2ed4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ed4 OCA], [~~http~~://pdbe.org/2ed4 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=2ed4 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/2ed4 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=2ed4 ProSAT], [~~http~~://www.topsan.org/Proteins/RSGI/2ed4 TOPSAN]</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=2ed4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ed4 OCA], [https://pdbe.org/2ed4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ed4 RCSB], [https://www.ebi.ac.uk/pdbsum/2ed4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ed4 ProSAT], [https://www.topsan.org/Proteins/RSGI/2ed4 TOPSAN]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[[~~http~~://www.uniprot.org/uniprot/HPAC_THET8 HPAC_THET8]] Catalyzes the reduction of free flavins (FMN, FAD and riboflavin) by NADH. Subsequently, the reduced flavins diffuse to the large HpaB component.<ref>PMID:17729270</ref>		[[https://www.uniprot.org/uniprot/HPAC_THET8 HPAC_THET8]] Catalyzes the reduction of free flavins (FMN, FAD and riboflavin) by NADH. Subsequently, the reduced flavins diffuse to the large HpaB component.<ref>PMID:17729270</ref>
	== 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: Large Structures]]
	[[Category: Thet8]]		[[Category: Thet8]]
	[[Category: Ebihara, A]]		[[Category: Ebihara, A]]

OCA at 06:47, 6 June 2018

2018-06-06T06:47:53Z

← Older revision		Revision as of 06:47, 6 June 2018
Line 1:		Line 1:

	==Crystal structure of flavin reductase HpaC complexed with FAD and NAD==		==Crystal structure of flavin reductase HpaC complexed with FAD and NAD==
	<StructureSection load='2ed4' size='340' side='right' caption='[[2ed4]], [[Resolution\|resolution]] 1.85Å' scene=''>		<StructureSection load='2ed4' size='340' side='right' caption='[[2ed4]], [[Resolution\|resolution]] 1.85Å' scene=''>
Line 6:		Line 7:
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2ecr\|2ecr]], [[2ecu\|2ecu]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2ecr\|2ecr]], [[2ecu\|2ecu]]</td></tr>
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">TTHA0961 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=300852 THET8])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">TTHA0961 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=300852 THET8])</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=2ed4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ed4 OCA], [http://pdbe.org/2ed4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2ed4 RCSB], [http://www.ebi.ac.uk/pdbsum/2ed4 PDBsum], [http://www.topsan.org/Proteins/RSGI/2ed4 TOPSAN]</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=2ed4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ed4 OCA], [http://pdbe.org/2ed4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2ed4 RCSB], [http://www.ebi.ac.uk/pdbsum/2ed4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2ed4 ProSAT], [http://www.topsan.org/Proteins/RSGI/2ed4 TOPSAN]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 14:		Line 15:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ed/2ed4_consurf.spt"</scriptWhenChecked>		<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ed/2ed4_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=2ed4 ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">

OCA at 07:42, 11 September 2015

2015-09-11T07:42:27Z

← Older revision		Revision as of 07:42, 11 September 2015
Line 2:		Line 2:
	<StructureSection load='2ed4' size='340' side='right' caption='[[2ed4]], [[Resolution\|resolution]] 1.85Å' scene=''>		<StructureSection load='2ed4' size='340' side='right' caption='[[2ed4]], [[Resolution\|resolution]] 1.85Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2ed4]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Thermus_thermophilus_hb8 Thermus thermophilus hb8~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ED4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ED4 FirstGlance]. <br>		<table><tr><td colspan='2'>[[2ed4]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Thet8 Thet8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ED4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ED4 FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2ecr\|2ecr]], [[2ecu\|2ecu]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2ecr\|2ecr]], [[2ecu\|2ecu]]</td></tr>
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">TTHA0961 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=300852 ~~Thermus thermophilus HB8~~])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">TTHA0961 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=300852 THET8])</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=2ed4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ed4 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2ed4 RCSB], [http://www.ebi.ac.uk/pdbsum/2ed4 PDBsum], [http://www.topsan.org/Proteins/RSGI/2ed4 TOPSAN]</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=2ed4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ed4 OCA], [http://pdbe.org/2ed4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2ed4 RCSB], [http://www.ebi.ac.uk/pdbsum/2ed4 PDBsum], [http://www.topsan.org/Proteins/RSGI/2ed4 TOPSAN]</span></td></tr>
	</table>		</table>
			== Function ==
			[[http://www.uniprot.org/uniprot/HPAC_THET8 HPAC_THET8]] Catalyzes the reduction of free flavins (FMN, FAD and riboflavin) by NADH. Subsequently, the reduced flavins diffuse to the large HpaB component.<ref>PMID:17729270</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 26:		Line 28:
	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 2ed4" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: ~~Thermus thermophilus hb8~~]]		[[Category: Thet8]]
	[[Category: Ebihara, A]]		[[Category: Ebihara, A]]
	[[Category: Hisano, T]]		[[Category: Hisano, T]]

OCA at 16:32, 15 January 2015

2015-01-15T16:32:02Z

← Older revision		Revision as of 16:32, 15 January 2015
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2ed4]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus_hb8 Thermus thermophilus hb8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ED4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ED4 FirstGlance]. <br>		<table><tr><td colspan='2'>[[2ed4]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus_hb8 Thermus thermophilus hb8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ED4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ED4 FirstGlance]. <br>
	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene><br>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene></td></tr>
	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2ecr\|2ecr]], [[2ecu\|2ecu]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2ecr\|2ecr]], [[2ecu\|2ecu]]</td></tr>
	<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">TTHA0961 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=300852 Thermus thermophilus HB8])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">TTHA0961 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=300852 Thermus thermophilus HB8])</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=2ed4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ed4 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2ed4 RCSB], [http://www.ebi.ac.uk/pdbsum/2ed4 PDBsum], [http://www.topsan.org/Proteins/RSGI/2ed4 TOPSAN]</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=2ed4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ed4 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2ed4 RCSB], [http://www.ebi.ac.uk/pdbsum/2ed4 PDBsum], [http://www.topsan.org/Proteins/RSGI/2ed4 TOPSAN]</span></td></tr>
	<table>		</table>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 31:		Line 31:
	</StructureSection>		</StructureSection>
	[[Category: Thermus thermophilus hb8]]		[[Category: Thermus thermophilus hb8]]
	[[Category: Ebihara, A.]]		[[Category: Ebihara, A]]
	[[Category: Hisano, T.]]		[[Category: Hisano, T]]
	[[Category: Iwasaki, W.]]		[[Category: Iwasaki, W]]
	[[Category: Kim, S H.]]		[[Category: Kim, S H]]
	[[Category: Miki, K.]]		[[Category: Miki, K]]
	[[Category: Flavin diffusible]]		[[Category: Flavin diffusible]]
	[[Category: Flavin reductase]]		[[Category: Flavin reductase]]
	[[Category: Oxidoreductase]]		[[Category: Oxidoreductase]]
	[[Category: Two-component monooxygenase]]		[[Category: Two-component monooxygenase]]

OCA at 00:05, 30 September 2014

2014-09-30T00:05:48Z

← Older revision		Revision as of 00:05, 30 September 2014
Line 1:		Line 1:
	[[Image:~~2ed4~~.~~png~~\|~~left~~\|~~200px~~]]		==Crystal structure of flavin reductase HpaC complexed with FAD and NAD==
			<StructureSection load='2ed4' size='340' side='right' caption='[[2ed4]], [[Resolution\|resolution]] 1.85Å' scene=''>
			== Structural highlights ==
			<table><tr><td colspan='2'>[[2ed4]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus_hb8 Thermus thermophilus hb8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ED4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ED4 FirstGlance]. <br>
			</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene><br>
			<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2ecr\|2ecr]], [[2ecu\|2ecu]]</td></tr>
			<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">TTHA0961 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=300852 Thermus thermophilus HB8])</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=2ed4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ed4 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2ed4 RCSB], [http://www.ebi.ac.uk/pdbsum/2ed4 PDBsum], [http://www.topsan.org/Proteins/RSGI/2ed4 TOPSAN]</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/ed/2ed4_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 two-component enzyme, 4-hydroxyphenylacetate 3-monooxygenase, catalyzes the conversion of 4-hydroxyphenylacetate to 3,4-dihydroxyphenylacetate. In the overall reaction, the oxygenase component (HpaB) introduces a hydroxyl group into the benzene ring of 4-hydroxyphenylacetate using molecular oxygen and reduced flavin, while the reductase component (HpaC) provides free reduced flavins for HpaB. The crystal structures of HpaC from Thermus thermophilus HB8 in the ligand-free form, the FAD-containing form, and the ternary complex with FAD and NAD(+) were determined. In the ligand-free form, two large grooves are present at the dimer interface, and are occupied by water molecules. A structural analysis of HpaC containing FAD revealed that FAD has a low occupancy, indicating that it is not tightly bound to HpaC. This was further confirmed in flavin dissociation experiments, showing that FAD can be released from HpaC. The structure of the ternary complex revealed that FAD and NAD(+) are bound in the groove in the extended and folded conformation, respectively. The nicotinamide ring of NAD(+) is sandwiched between the adenine ring of NAD(+) and the isoalloxazine ring of FAD. The distance between N5 of the isoalloxazine ring and C4 of the nicotinamide ring is about 3.3 A, sufficient to permit hydride transfer. The structures of these three states are essentially identical, however, the side chains of several residues show small conformational changes, indicating an induced fit upon binding of NADH. Inactivity with respect to NADPH can be explained as instability of the binding of NADPH with the negatively charged 2'-phosphate group buried inside the complex, as well as a possible repulsive effect by the dipole of helix alpha1. A comparison of the binding mode of FAD with that in PheA2 from Bacillus thermoglucosidasius A7, which contains FAD as a prosthetic group, reveals remarkable conformational differences in a less conserved loop region (Gly83-Gly94) involved in the binding of the AMP moiety of FAD. These data suggest that variations in the affinities for FAD in the reductases of the two-component flavin-diffusible monooxygenase family may be attributed to difference in the interaction between the AMP moiety of FAD and the less conserved loop region which possibly shows structural divergence.

	~~{{STRUCTURE_2ed4\| PDB=2ed4 \| SCENE= }}~~		Crystal structure of the flavin reductase component (HpaC) of 4-hydroxyphenylacetate 3-monooxygenase from Thermus thermophilus HB8: Structural basis for the flavin affinity.,Kim SH, Hisano T, Iwasaki W, Ebihara A, Miki K Proteins. 2008 Feb 15;70(3):718-30. PMID:17729270<ref>PMID:17729270</ref>

	~~===Crystal structure~~ of ~~flavin reductase HpaC complexed with FAD and NAD===~~		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
			</div>
	~~{{ABSTRACT_PUBMED_17729270}}~~		== References ==
			<references/>
	~~==About this Structure==~~		__TOC__
	~~[[2ed4]] is a 2 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Thermus_thermophilus_hb8 Thermus thermophilus hb8]~~. ~~Full crystallographic information is available from [http:~~/~~/oca.weizmann.ac.il/oca-bin/ocashort?id=2ED4 OCA].~~		</StructureSection>

	==~~Reference~~==
	<~~ref group="xtra">PMID:017729270<~~/~~ref~~><~~references group="xtra"~~/>
	[[Category: Thermus thermophilus hb8]]		[[Category: Thermus thermophilus hb8]]
	[[Category: Ebihara, A.]]		[[Category: Ebihara, A.]]

OCA: Protected "2ed4" [edit=sysop:move=sysop]

2013-01-06T09:32:25Z

Protected "2ed4" [edit=sysop:move=sysop]

← Older revision	Revision as of 09:32, 6 January 2013
(No difference)

OCA at 09:32, 6 January 2013

2013-01-06T09:32:21Z

← Older revision		Revision as of 09:32, 6 January 2013
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	~~{{Seed}}~~
	[[Image:2ed4.png\|left\|200px]]		[[Image:2ed4.png\|left\|200px]]

	~~<!--~~
	~~The line below this paragraph, containing "STRUCTURE_2ed4", 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_2ed4\| PDB=2ed4 \| SCENE= }}		{{STRUCTURE_2ed4\| PDB=2ed4 \| SCENE= }}

	===Crystal structure of flavin reductase HpaC complexed with FAD and NAD===		===Crystal structure of flavin reductase HpaC complexed with FAD and NAD===


	~~<!--~~
	~~The line below this paragraph, {{ABSTRACT_PUBMED_17729270}}, adds the Publication Abstract to the page~~
	~~(as it appears on PubMed at http://www.pubmed.gov), where 17729270 is the PubMed ID number.~~
	~~-->~~
	{{ABSTRACT_PUBMED_17729270}}		{{ABSTRACT_PUBMED_17729270}}

	==About this Structure==		==About this Structure==
	~~2ED4~~ is a 2 ~~chains~~ structure ~~of sequences~~ from [http://en.wikipedia.org/wiki/~~Thermus_thermophilus~~ Thermus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ED4 OCA].		[[2ed4]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus_hb8 Thermus thermophilus hb8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ED4 OCA].

	==Reference==		==Reference==
	<ref group="xtra">PMID:~~17729270~~</ref><references group="xtra"/>		<ref group="xtra">PMID:017729270</ref><references group="xtra"/>
	[[Category: Thermus thermophilus]]		[[Category: Thermus thermophilus hb8]]
	[[Category: Ebihara, A.]]		[[Category: Ebihara, A.]]
	[[Category: Hisano, T.]]		[[Category: Hisano, T.]]
Line 34:		Line 22:
	[[Category: Oxidoreductase]]		[[Category: Oxidoreductase]]
	[[Category: Two-component monooxygenase]]		[[Category: Two-component monooxygenase]]
	~~[[Category: X-ray diffraction]]~~

	~~''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 17:19:07 2009''~~

OCA at 15:19, 17 February 2009

2009-02-17T15:19:09Z

← Older revision		Revision as of 15:19, 17 February 2009
Line 23:		Line 23:

	==Reference==		==Reference==
	Crystal structure of the flavin reductase component (HpaC) of 4-hydroxyphenylacetate 3-monooxygenase from Thermus thermophilus HB8: Structural basis for the flavin affinity., Kim SH, Hisano T, Iwasaki W, Ebihara A, Miki K, Proteins. 2008 Feb 15;70(3):718-30. PMID:~~[http://www.ncbi.nlm.nih.gov~~/~~pubmed~~/~~17729270 17729270]~~		<ref group="xtra">PMID:17729270</ref><references group="xtra"/>
	[[Category: Thermus thermophilus]]		[[Category: Thermus thermophilus]]
	[[Category: Ebihara, A.]]		[[Category: Ebihara, A.]]
Line 36:		Line 36:
	[[Category: X-ray diffraction]]		[[Category: X-ray diffraction]]

	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sun Nov 16 15~~:08:~~05 2008~~''		''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 17:19:07 2009''

OCA at 13:08, 16 November 2008

2008-11-16T13:08:09Z

← Older revision		Revision as of 13:08, 16 November 2008
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	==About this Structure==		==About this Structure==
	2ED4 is a ~~[[Single protein]]~~ structure of ~~sequence~~ from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ED4 OCA].		2ED4 is a 2 chains structure of sequences from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ED4 OCA].

	==Reference==		==Reference==
	Crystal structure of the flavin reductase component (HpaC) of 4-hydroxyphenylacetate 3-monooxygenase from Thermus thermophilus HB8: Structural basis for the flavin affinity., Kim SH, Hisano T, Iwasaki W, Ebihara A, Miki K, Proteins. 2008 Feb 15;70(3):718-30. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17729270 17729270]		Crystal structure of the flavin reductase component (HpaC) of 4-hydroxyphenylacetate 3-monooxygenase from Thermus thermophilus HB8: Structural basis for the flavin affinity., Kim SH, Hisano T, Iwasaki W, Ebihara A, Miki K, Proteins. 2008 Feb 15;70(3):718-30. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17729270 17729270]
	~~[[Category: Single protein]]~~
	[[Category: Thermus thermophilus]]		[[Category: Thermus thermophilus]]
	[[Category: Ebihara, A.]]		[[Category: Ebihara, A.]]
Line 37:		Line 36:
	[[Category: X-ray diffraction]]		[[Category: X-ray diffraction]]

	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Tue Jul 29 00~~:12:39 2008''		''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Nov 16 15:08:05 2008''