4o93 - Revision history

OCA at 12:38, 1 March 2024

OCA — Fri, 01 Mar 2024 12:38:22 GMT

←Older revision		Revision as of 12:38, 1 March 2024
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4o93]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_thermophilus_HB27 Thermus thermophilus HB27]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4O93 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4O93 FirstGlance]. <br>		<table><tr><td colspan='2'>[[4o93]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_thermophilus_HB27 Thermus thermophilus HB27]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4O93 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4O93 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</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]] 2.77Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</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=4o93 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4o93 OCA], [https://pdbe.org/4o93 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4o93 RCSB], [https://www.ebi.ac.uk/pdbsum/4o93 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4o93 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=4o93 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4o93 OCA], [https://pdbe.org/4o93 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4o93 RCSB], [https://www.ebi.ac.uk/pdbsum/4o93 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4o93 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[https://www.uniprot.org/uniprot/Q72GR9_THET2 Q72GR9_THET2]		[https://www.uniprot.org/uniprot/Q72GR9_THET2 Q72GR9_THET2]
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	NADPH/NADP(+) (the reduced form of NADP(+)/nicotinamide adenine dinucleotide phosphate) homeostasis is critical for countering oxidative stress in cells. Nicotinamide nucleotide transhydrogenase (TH), a membrane enzyme present in both bacteria and mitochondria, couples the proton motive force to the generation of NADPH. We present the 2.8 A crystal structure of the transmembrane proton channel domain of TH from Thermus thermophilus and the 6.9 A crystal structure of the entire enzyme (holo-TH). The membrane domain crystallized as a symmetric dimer, with each protomer containing a putative proton channel. The holo-TH is a highly asymmetric dimer with the NADP(H)-binding domain (dIII) in two different orientations. This unusual arrangement suggests a catalytic mechanism in which the two copies of dIII alternatively function in proton translocation and hydride transfer.
-
-	Structural biology. Division of labor in transhydrogenase by alternating proton translocation and hydride transfer.,Leung JH, Schurig-Briccio LA, Yamaguchi M, Moeller A, Speir JA, Gennis RB, Stout CD Science. 2015 Jan 9;347(6218):178-81. doi: 10.1126/science.1260451. PMID:25574024<ref>PMID:25574024</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 4o93" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
	*[[NAD(P) transhydrogenase 3D structures\|NAD(P) transhydrogenase 3D structures]]		*[[NAD(P) transhydrogenase 3D structures\|NAD(P) transhydrogenase 3D structures]]
-	== References ==
-	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>

OCA at 07:12, 25 January 2023

OCA — Wed, 25 Jan 2023 07:12:26 GMT

←Older revision		Revision as of 07:12, 25 January 2023
Line 3:		Line 3:
	<StructureSection load='4o93' size='340' side='right'caption='[[4o93]], [[Resolution\|resolution]] 2.77Å' scene=''>		<StructureSection load='4o93' size='340' side='right'caption='[[4o93]], [[Resolution\|resolution]] 2.77Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4o93]] is a 4 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Thet2 Thet2~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4O93 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4O93 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4o93]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_thermophilus_HB27 Thermus thermophilus HB27]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4O93 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4O93 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</scene~~></td></tr>~~	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</scene></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">TT_C1779 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=262724 THET2]), TT_C1778 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=262724 THET2])</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=4o93 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4o93 OCA], [https://pdbe.org/4o93 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4o93 RCSB], [https://www.ebi.ac.uk/pdbsum/4o93 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4o93 ProSAT]</span></td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/NAD(P)(+)_transhydrogenase_(Re/Si-specific) NAD(P)(+) transhydrogenase (Re/Si-specific)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.6.1.2 1.6.1.2] </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=4o93 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4o93 OCA], [~~http~~://pdbe.org/4o93 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4o93 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4o93 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4o93 ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/Q72GS0_THET2 Q72GS0_THET2]] The transhydrogenation between NADH and NADP is coupled to respiration and ATP hydrolysis and functions as a proton pump across the membrane (By similarity).[PIRNR:PIRNR000204]	+	[https://www.uniprot.org/uniprot/Q72GR9_THET2 Q72GR9_THET2]
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 22:		Line 20:

	==See Also==		==See Also==
-	*[[NAD(P) transhydrogenase\|NAD(P) transhydrogenase]]	+	*[[NAD(P) transhydrogenase 3D structures\|NAD(P) transhydrogenase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
Line 28:		Line 26:
	</StructureSection>		</StructureSection>
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: ~~Thet2~~]]	+	[[Category: Thermus thermophilus HB27]]
-	[[Category: Carragher, B]]	+	[[Category: Carragher B]]
-	[[Category: Gennis~~, R B~~]]	+	[[Category: Gennis RB]]
-	[[Category: Leung~~, J H~~]]	+	[[Category: Leung JH]]
-	[[Category: Moeller, A]]	+	[[Category: Moeller A]]
-	[[Category: Potter~~, C S~~]]	+	[[Category: Potter CS]]
-	[[Category: Schurig-Briccio~~, L A~~]]	+	[[Category: Schurig-Briccio LA]]
-	[[Category: Stout~~, C D~~]]	+	[[Category: Stout CD]]
-	[[Category: Yamaguchi, M]]	+	[[Category: Yamaguchi M]]
-	~~[[Category: Membrane domain dimer]]~~	+
-	~~[[Category: Membrane protein~~]]	+

OCA at 08:50, 10 April 2019

OCA — Wed, 10 Apr 2019 08:50:24 GMT

←Older revision		Revision as of 08:50, 10 April 2019
Line 1:		Line 1:

	==Crystal structure of Thermus thermophilis transhydrogeanse domain II dimer==		==Crystal structure of Thermus thermophilis transhydrogeanse domain II dimer==
-	<StructureSection load='4o93' size='340' side='right' caption='[[4o93]], [[Resolution\|resolution]] 2.77Å' scene=''>	+	<StructureSection load='4o93' size='340' side='right'caption='[[4o93]], [[Resolution\|resolution]] 2.77Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4o93]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4O93 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4O93 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4o93]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Thet2 Thet2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4O93 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4O93 FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</scene></td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">TT_C1779 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=262724 THET2]), TT_C1778 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=262724 THET2])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/NAD(P)(+)_transhydrogenase_(Re/Si-specific) NAD(P)(+) transhydrogenase (Re/Si-specific)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.6.1.2 1.6.1.2] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/NAD(P)(+)_transhydrogenase_(Re/Si-specific) NAD(P)(+) transhydrogenase (Re/Si-specific)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.6.1.2 1.6.1.2] </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=4o93 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4o93 OCA], [http://pdbe.org/4o93 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4o93 RCSB], [http://www.ebi.ac.uk/pdbsum/4o93 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4o93 ProSAT]</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=4o93 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4o93 OCA], [http://pdbe.org/4o93 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4o93 RCSB], [http://www.ebi.ac.uk/pdbsum/4o93 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4o93 ProSAT]</span></td></tr>
Line 26:		Line 27:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Large Structures]]
		+	[[Category: Thet2]]
	[[Category: Carragher, B]]		[[Category: Carragher, B]]
	[[Category: Gennis, R B]]		[[Category: Gennis, R B]]

OCA at 12:05, 11 August 2016

OCA — Thu, 11 Aug 2016 12:05:07 GMT

←Older revision		Revision as of 12:05, 11 August 2016
Line 1:		Line 1:
		+
	==Crystal structure of Thermus thermophilis transhydrogeanse domain II dimer==		==Crystal structure of Thermus thermophilis transhydrogeanse domain II dimer==
	<StructureSection load='4o93' size='340' side='right' caption='[[4o93]], [[Resolution\|resolution]] 2.77Å' scene=''>		<StructureSection load='4o93' size='340' side='right' caption='[[4o93]], [[Resolution\|resolution]] 2.77Å' scene=''>
Line 5:		Line 6:
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</scene></td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/NAD(P)(+)_transhydrogenase_(Re/Si-specific) NAD(P)(+) transhydrogenase (Re/Si-specific)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.6.1.2 1.6.1.2] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/NAD(P)(+)_transhydrogenase_(Re/Si-specific) NAD(P)(+) transhydrogenase (Re/Si-specific)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.6.1.2 1.6.1.2] </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=4o93 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4o93 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4o93 RCSB], [http://www.ebi.ac.uk/pdbsum/4o93 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=4o93 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4o93 OCA], [http://pdbe.org/4o93 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4o93 RCSB], [http://www.ebi.ac.uk/pdbsum/4o93 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4o93 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 17:		Line 18:
	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 4o93" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[NAD(P) transhydrogenase\|NAD(P) transhydrogenase]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 11:04, 28 January 2015

OCA — Wed, 28 Jan 2015 11:04:16 GMT

←Older revision		Revision as of 11:04, 28 January 2015
Line 9:		Line 9:
	== Function ==		== Function ==
	[[http://www.uniprot.org/uniprot/Q72GS0_THET2 Q72GS0_THET2]] The transhydrogenation between NADH and NADP is coupled to respiration and ATP hydrolysis and functions as a proton pump across the membrane (By similarity).[PIRNR:PIRNR000204]		[[http://www.uniprot.org/uniprot/Q72GS0_THET2 Q72GS0_THET2]] The transhydrogenation between NADH and NADP is coupled to respiration and ATP hydrolysis and functions as a proton pump across the membrane (By similarity).[PIRNR:PIRNR000204]
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	NADPH/NADP(+) (the reduced form of NADP(+)/nicotinamide adenine dinucleotide phosphate) homeostasis is critical for countering oxidative stress in cells. Nicotinamide nucleotide transhydrogenase (TH), a membrane enzyme present in both bacteria and mitochondria, couples the proton motive force to the generation of NADPH. We present the 2.8 A crystal structure of the transmembrane proton channel domain of TH from Thermus thermophilus and the 6.9 A crystal structure of the entire enzyme (holo-TH). The membrane domain crystallized as a symmetric dimer, with each protomer containing a putative proton channel. The holo-TH is a highly asymmetric dimer with the NADP(H)-binding domain (dIII) in two different orientations. This unusual arrangement suggests a catalytic mechanism in which the two copies of dIII alternatively function in proton translocation and hydride transfer.
		+
		+	Structural biology. Division of labor in transhydrogenase by alternating proton translocation and hydride transfer.,Leung JH, Schurig-Briccio LA, Yamaguchi M, Moeller A, Speir JA, Gennis RB, Stout CD Science. 2015 Jan 9;347(6218):178-81. doi: 10.1126/science.1260451. PMID:25574024<ref>PMID:25574024</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	== References ==
		+	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>

OCA at 14:51, 31 December 2014

OCA — Wed, 31 Dec 2014 14:51:28 GMT

←Older revision		Revision as of 14:51, 31 December 2014
Line 1:		Line 1:
-	'''~~Unreleased structure~~'''	+	==Crystal structure of Thermus thermophilis transhydrogeanse domain II dimer==
-		+	<StructureSection load='4o93' size='340' side='right' caption='[[4o93]], [[Resolution\|resolution]] 2.77Å' scene=''>
-	~~The entry~~ 4o93 is ~~ON HOLD until Paper Publication~~	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[4o93]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4O93 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4O93 FirstGlance]. <br>
-	~~Authors~~: ~~Leung, J~~.H.~~, Yamaguchi, M~~.~~, Moeller, A., Schurig~~-~~Briccio, L~~.A.~~, Gennis, R~~.B.~~, Potter, C~~.~~S., Carragher, B., Stout, C.D~~.	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</scene></td></tr>
-		+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/NAD(P)(+)_transhydrogenase_(Re/Si-specific) NAD(P)(+) transhydrogenase (Re/Si-specific)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.6.1.2 1.6.1.2] </span></td></tr>
-	~~Description: Crystal structure of Thermus thermophilis transhydrogeanse domain II dimer~~	+	<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=4o93 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4o93 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4o93 RCSB], [http://www.ebi.ac.uk/pdbsum/4o93 PDBsum]</span></td></tr>
-	[[~~Category~~: ~~Unreleased Structures~~]]	+	</table>
-	[~~[Category~~: ~~Gennis~~, R.B]]	+	== Function ==
-	[[~~Category~~: ~~Schurig~~-~~Briccio~~, L.A]]	+	[[http://www.uniprot.org/uniprot/Q72GS0_THET2 Q72GS0_THET2]] The transhydrogenation between NADH and NADP is coupled to respiration and ATP hydrolysis and functions as a proton pump across the membrane (By similarity).[PIRNR:PIRNR000204]
-	[[~~Category~~: ~~Leung, J~~.H]]	+	__TOC__
		+	</StructureSection>
	[[Category: Carragher, B]]		[[Category: Carragher, B]]
-	[[Category: ~~Yamaguchi~~, M]]	+	[[Category: Gennis, R B]]
		+	[[Category: Leung, J H]]
	[[Category: Moeller, A]]		[[Category: Moeller, A]]
-	[[Category: Potter, C.S]]	+	[[Category: Potter, C S]]
-	[[Category: Stout, C.D]]	+	[[Category: Schurig-Briccio, L A]]
		+	[[Category: Stout, C D]]
		+	[[Category: Yamaguchi, M]]
		+	[[Category: Membrane domain dimer]]
		+	[[Category: Membrane protein]]

OCA at 14:19, 24 December 2014

OCA — Wed, 24 Dec 2014 14:19:23 GMT

←Older revision		Revision as of 14:19, 24 December 2014
Line 6:		Line 6:

	Description: Crystal structure of Thermus thermophilis transhydrogeanse domain II dimer		Description: Crystal structure of Thermus thermophilis transhydrogeanse domain II dimer
		+	[[Category: Unreleased Structures]]
		+	[[Category: Gennis, R.B]]
		+	[[Category: Schurig-Briccio, L.A]]
		+	[[Category: Leung, J.H]]
		+	[[Category: Carragher, B]]
		+	[[Category: Yamaguchi, M]]
		+	[[Category: Moeller, A]]
		+	[[Category: Potter, C.S]]
		+	[[Category: Stout, C.D]]

OCA at 08:58, 16 April 2014

OCA — Wed, 16 Apr 2014 08:58:14 GMT

←Older revision		Revision as of 08:58, 16 April 2014
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 4o93 is ON HOLD	+	The entry 4o93 is ON HOLD until Paper Publication

	Authors: Leung, J.H., Yamaguchi, M., Moeller, A., Schurig-Briccio, L.A., Gennis, R.B., Potter, C.S., Carragher, B., Stout, C.D.		Authors: Leung, J.H., Yamaguchi, M., Moeller, A., Schurig-Briccio, L.A., Gennis, R.B., Potter, C.S., Carragher, B., Stout, C.D.

	Description: Crystal structure of Thermus thermophilis transhydrogeanse domain II dimer		Description: Crystal structure of Thermus thermophilis transhydrogeanse domain II dimer

OCA: Protected "4o93" [edit=sysop:move=sysop]

OCA — Wed, 08 Jan 2014 09:29:02 GMT

Protected "4o93" [edit=sysop:move=sysop]

←Older revision

Revision as of 09:29, 8 January 2014

OCA: New page: '''Unreleased structure''' The entry 4o93 is ON HOLD Authors: Leung, J.H., Yamaguchi, M., Moeller, A., Schurig-Briccio, L.A., Gennis, R.B., Potter, C.S., Carragher, B., Stout, C.D. Des...

OCA — Wed, 08 Jan 2014 09:29:01 GMT

New page: '''Unreleased structure''' The entry 4o93 is ON HOLD Authors: Leung, J.H., Yamaguchi, M., Moeller, A., Schurig-Briccio, L.A., Gennis, R.B., Potter, C.S., Carragher, B., Stout, C.D. Des...

New page

'''Unreleased structure'''

The entry 4o93 is ON HOLD

Authors: Leung, J.H., Yamaguchi, M., Moeller, A., Schurig-Briccio, L.A., Gennis, R.B., Potter, C.S., Carragher, B., Stout, C.D.

Description: Crystal structure of Thermus thermophilis transhydrogeanse domain II dimer