3rox - Revision history

OCA at 10:24, 6 November 2024

2024-11-06T10:24:22Z

← Older revision		Revision as of 10:24, 6 November 2024
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	== Function ==		== Function ==
	[https://www.uniprot.org/uniprot/NNRE_MOUSE NNRE_MOUSE] Catalyzes the epimerization of the S- and R-forms of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. This is a prerequisite for the S-specific NAD(P)H-hydrate dehydratase to allow the repair of both epimers of NAD(P)HX.[HAMAP-Rule:MF_03159]<ref>PMID:21994945</ref>		[https://www.uniprot.org/uniprot/NNRE_MOUSE NNRE_MOUSE] Catalyzes the epimerization of the S- and R-forms of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. This is a prerequisite for the S-specific NAD(P)H-hydrate dehydratase to allow the repair of both epimers of NAD(P)HX.[HAMAP-Rule:MF_03159]<ref>PMID:21994945</ref>
			<div style="background-color:#fffaf0;">
			== Publication Abstract from PubMed ==
			Proteins of unknown function comprise a significant fraction of sequenced genomes. Defining the roles of these proteins is vital to understanding cellular processes. Here, we describe a method to determine a protein function based on the identification of its natural ligand(s) by the crystallographic screening of the binding of a metabolite library, followed by a focused search in the metabolic space. The method was applied to two protein families with unknown function, PF01256 and YjeF_N. The PF01256 proteins, represented by YxkO from Bacillus subtilis and the C-terminal domain of Tm0922 from Thermotoga maritima, were shown to catalyze ADP/ATP-dependent NAD(P)H-hydrate dehydratation, a previously described orphan activity. The YjeF_N proteins, represented by mouse apolipoprotein A-I binding protein and the N-terminal domain of Tm0922, were found to interact with an adenosine diphosphoribose-related substrate and likely serve as ADP-ribosyltransferases. Crystallographic screening of metabolites serves as an efficient tool in functional analyses of uncharacterized proteins.

			Identification of Unknown Protein Function Using Metabolite Cocktail Screening.,Shumilin IA, Cymborowski M, Chertihin O, Jha KN, Herr JC, Lesley SA, Joachimiak A, Minor W Structure. 2012 Aug 28. PMID:22940582<ref>PMID:22940582</ref>

			From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
			</div>
			<div class="pdbe-citations 3rox" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 12:32, 14 March 2024

2024-03-14T12:32:20Z

← Older revision		Revision as of 12:32, 14 March 2024
Line 10:		Line 10:
	== Function ==		== Function ==
	[https://www.uniprot.org/uniprot/NNRE_MOUSE NNRE_MOUSE] Catalyzes the epimerization of the S- and R-forms of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. This is a prerequisite for the S-specific NAD(P)H-hydrate dehydratase to allow the repair of both epimers of NAD(P)HX.[HAMAP-Rule:MF_03159]<ref>PMID:21994945</ref>		[https://www.uniprot.org/uniprot/NNRE_MOUSE NNRE_MOUSE] Catalyzes the epimerization of the S- and R-forms of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. This is a prerequisite for the S-specific NAD(P)H-hydrate dehydratase to allow the repair of both epimers of NAD(P)HX.[HAMAP-Rule:MF_03159]<ref>PMID:21994945</ref>
	~~<div style="background-color:#fffaf0;">~~
	~~== Publication Abstract from PubMed ==~~
	Proteins of unknown function comprise a significant fraction of sequenced genomes. Defining the roles of these proteins is vital to understanding cellular processes. Here, we describe a method to determine a protein function based on the identification of its natural ligand(s) by the crystallographic screening of the binding of a metabolite library, followed by a focused search in the metabolic space. The method was applied to two protein families with unknown function, PF01256 and YjeF_N. The PF01256 proteins, represented by YxkO from Bacillus subtilis and the C-terminal domain of Tm0922 from Thermotoga maritima, were shown to catalyze ADP/ATP-dependent NAD(P)H-hydrate dehydratation, a previously described orphan activity. The YjeF_N proteins, represented by mouse apolipoprotein A-I binding protein and the N-terminal domain of Tm0922, were found to interact with an adenosine diphosphoribose-related substrate and likely serve as ADP-ribosyltransferases. Crystallographic screening of metabolites serves as an efficient tool in functional analyses of uncharacterized proteins.

	Identification of Unknown Protein Function Using Metabolite Cocktail Screening.,Shumilin IA, Cymborowski M, Chertihin O, Jha KN, Herr JC, Lesley SA, Joachimiak A, Minor W Structure. 2012 Aug 28. PMID:22940582<ref>PMID:22940582</ref>

	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~
	~~</div>~~
	~~<div class="pdbe-citations 3rox" style="background-color:#fffaf0;"></div>~~
	== References ==		== References ==
	<references/>		<references/>

OCA at 08:14, 6 December 2023

2023-12-06T08:14:39Z

← Older revision		Revision as of 08:14, 6 December 2023
Line 3:		Line 3:
	<StructureSection load='3rox' size='340' side='right'caption='[[3rox]], [[Resolution\|resolution]] 2.40Å' scene=''>		<StructureSection load='3rox' size='340' side='right'caption='[[3rox]], [[Resolution\|resolution]] 2.40Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[3rox]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Lk3_transgenic_mice Lk3 transgenic mice~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ROX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ROX FirstGlance]. <br>		<table><tr><td colspan='2'>[[3rox]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ROX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ROX FirstGlance]. <br>
	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>~~, ~~<scene name='pdbligand=TEP:THEOPHYLLINE'>TEP</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]] 2.4Å</td></tr>
	<tr id='~~NonStdRes~~'><td class="sblockLbl"><b>[[~~Non-Standard_Residue~~\|~~NonStd Res~~:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene><~~/td></tr>~~		<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=TEP:THEOPHYLLINE'>TEP</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;'~~>~~[[2o8n\|2o8n]], [[2dg2\|2dg2]], [[3rno\|3rno]], [[3ro7\|3ro7]], [[3roe\|3roe]]~~, ~~[[3rog\|3rog]], [[3roz\|3roz]]~~<~~/div></td></tr>~~
	~~<tr id~~='~~gene'><td class~~=~~"sblockLbl"><b>[[Gene\|Gene~~:~~]]</b~~></~~td><td class="sblockDat"~~>~~Aibp, Apoa1bp ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])~~</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=3rox FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rox OCA], [https://pdbe.org/3rox PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3rox RCSB], [https://www.ebi.ac.uk/pdbsum/3rox PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3rox 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=3rox FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rox OCA], [https://pdbe.org/3rox PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3rox RCSB], [https://www.ebi.ac.uk/pdbsum/3rox PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3rox ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[[https://www.uniprot.org/uniprot/NNRE_MOUSE NNRE_MOUSE]] Catalyzes the epimerization of the S- and R-forms of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. This is a prerequisite for the S-specific NAD(P)H-hydrate dehydratase to allow the repair of both epimers of NAD(P)HX.[HAMAP-Rule:MF_03159]<ref>PMID:21994945</ref>		[https://www.uniprot.org/uniprot/NNRE_MOUSE NNRE_MOUSE] Catalyzes the epimerization of the S- and R-forms of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. This is a prerequisite for the S-specific NAD(P)H-hydrate dehydratase to allow the repair of both epimers of NAD(P)HX.[HAMAP-Rule:MF_03159]<ref>PMID:21994945</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 26:		Line 24:
	</StructureSection>		</StructureSection>
	[[Category: Large Structures]]		[[Category: Large Structures]]
	[[Category: ~~Lk3 transgenic mice~~]]		[[Category: Mus musculus]]
	[[Category: Cymborowski, M]]		[[Category: Cymborowski M]]
	[[Category: Herr~~, J C~~]]		[[Category: Herr JC]]
	[[Category: Jha~~, K N~~]]		[[Category: Jha KN]]
	[[Category: Minor, W]]		[[Category: Minor W]]
	[[Category: Shumilin~~, I A]]~~		[[Category: Shumilin IA]]
	~~[[Category: Protein binding]]~~
	~~[[Category: Rossmann fold~~]]

OCA at 09:57, 13 April 2022

2022-04-13T09:57:56Z

← Older revision		Revision as of 09:57, 13 April 2022
Line 1:		Line 1:

	==Crystal Structure of Mouse Apolipoprotein A-I Binding Protein in Complex with Theophylline==		==Crystal Structure of Mouse Apolipoprotein A-I Binding Protein in Complex with Theophylline==
	<StructureSection load='3rox' size='340' side='right' caption='[[3rox]], [[Resolution\|resolution]] 2.40Å' scene=''>		<StructureSection load='3rox' size='340' side='right'caption='[[3rox]], [[Resolution\|resolution]] 2.40Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[3rox]] is a 1 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ROX OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=3ROX FirstGlance]. <br>		<table><tr><td colspan='2'>[[3rox]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ROX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ROX FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=TEP:THEOPHYLLINE'>TEP</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=TEP:THEOPHYLLINE'>TEP</scene></td></tr>
	<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>		<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2o8n\|2o8n]], [[2dg2\|2dg2]], [[3rno\|3rno]], [[3ro7\|3ro7]], [[3roe\|3roe]], [[3rog\|3rog]], [[3roz\|3roz]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2o8n\|2o8n]], [[2dg2\|2dg2]], [[3rno\|3rno]], [[3ro7\|3ro7]], [[3roe\|3roe]], [[3rog\|3rog]], [[3roz\|3roz]]</div></td></tr>
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">Aibp, Apoa1bp ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">Aibp, Apoa1bp ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</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=3rox FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rox OCA], [~~http~~://pdbe.org/3rox PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=3rox RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/3rox PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=3rox 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=3rox FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rox OCA], [https://pdbe.org/3rox PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3rox RCSB], [https://www.ebi.ac.uk/pdbsum/3rox PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3rox ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[[~~http~~://www.uniprot.org/uniprot/NNRE_MOUSE NNRE_MOUSE]] Catalyzes the epimerization of the S- and R-forms of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. This is a prerequisite for the S-specific NAD(P)H-hydrate dehydratase to allow the repair of both epimers of NAD(P)HX.[HAMAP-Rule:MF_03159]<ref>PMID:21994945</ref>		[[https://www.uniprot.org/uniprot/NNRE_MOUSE NNRE_MOUSE]] Catalyzes the epimerization of the S- and R-forms of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. This is a prerequisite for the S-specific NAD(P)H-hydrate dehydratase to allow the repair of both epimers of NAD(P)HX.[HAMAP-Rule:MF_03159]<ref>PMID:21994945</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 25:		Line 25:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
			[[Category: Large Structures]]
	[[Category: Lk3 transgenic mice]]		[[Category: Lk3 transgenic mice]]
	[[Category: Cymborowski, M]]		[[Category: Cymborowski, M]]

OCA at 10:38, 5 August 2016

2016-08-05T10:38:44Z

← Older revision		Revision as of 10:38, 5 August 2016
Line 1:		Line 1:

	==Crystal Structure of Mouse Apolipoprotein A-I Binding Protein in Complex with Theophylline==		==Crystal Structure of Mouse Apolipoprotein A-I Binding Protein in Complex with Theophylline==
	<StructureSection load='3rox' size='340' side='right' caption='[[3rox]], [[Resolution\|resolution]] 2.40Å' scene=''>		<StructureSection load='3rox' size='340' side='right' caption='[[3rox]], [[Resolution\|resolution]] 2.40Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[3rox]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Mus_musculus Mus musculus~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ROX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ROX FirstGlance]. <br>		<table><tr><td colspan='2'>[[3rox]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ROX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ROX FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=TEP:THEOPHYLLINE'>TEP</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=TEP:THEOPHYLLINE'>TEP</scene></td></tr>
	<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>		<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2o8n\|2o8n]], [[2dg2\|2dg2]], [[3rno\|3rno]], [[3ro7\|3ro7]], [[3roe\|3roe]], [[3rog\|3rog]], [[3roz\|3roz]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2o8n\|2o8n]], [[2dg2\|2dg2]], [[3rno\|3rno]], [[3ro7\|3ro7]], [[3roe\|3roe]], [[3rog\|3rog]], [[3roz\|3roz]]</td></tr>
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">Aibp, Apoa1bp ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 ~~Mus musculus~~])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">Aibp, Apoa1bp ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</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=3rox FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rox OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3rox RCSB], [http://www.ebi.ac.uk/pdbsum/3rox 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=3rox FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rox OCA], [http://pdbe.org/3rox PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3rox RCSB], [http://www.ebi.ac.uk/pdbsum/3rox PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3rox ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[[http://www.uniprot.org/uniprot/~~AIBP_MOUSE AIBP_MOUSE~~]] Catalyzes the epimerization of the S- and R-forms of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. This is a prerequisite for the S-specific NAD(P)H-hydrate dehydratase to allow the repair of both epimers of NAD(P)HX.[HAMAP-Rule:MF_03159]<ref>PMID:21994945</ref>		[[http://www.uniprot.org/uniprot/NNRE_MOUSE NNRE_MOUSE]] Catalyzes the epimerization of the S- and R-forms of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. This is a prerequisite for the S-specific NAD(P)H-hydrate dehydratase to allow the repair of both epimers of NAD(P)HX.[HAMAP-Rule:MF_03159]<ref>PMID:21994945</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 19:		Line 20:
	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 3rox" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: ~~Mus musculus~~]]		[[Category: Lk3 transgenic mice]]
	[[Category: Cymborowski, M]]		[[Category: Cymborowski, M]]
	[[Category: Herr, J C]]		[[Category: Herr, J C]]

OCA at 01:39, 25 December 2014

2014-12-25T01:39:44Z

← Older revision		Revision as of 01:39, 25 December 2014
Line 9:		Line 9:
	<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=3rox FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rox OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3rox RCSB], [http://www.ebi.ac.uk/pdbsum/3rox 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=3rox FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rox OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3rox RCSB], [http://www.ebi.ac.uk/pdbsum/3rox PDBsum]</span></td></tr>
	</table>		</table>
			== Function ==
			[[http://www.uniprot.org/uniprot/AIBP_MOUSE AIBP_MOUSE]] Catalyzes the epimerization of the S- and R-forms of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. This is a prerequisite for the S-specific NAD(P)H-hydrate dehydratase to allow the repair of both epimers of NAD(P)HX.[HAMAP-Rule:MF_03159]<ref>PMID:21994945</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==

OCA at 10:46, 9 December 2014

2014-12-09T10:46:48Z

← Older revision		Revision as of 10:46, 9 December 2014
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	[[~~Image~~:~~3rox~~.~~png~~\|~~left~~\|~~200px~~]]		==Crystal Structure of Mouse Apolipoprotein A-I Binding Protein in Complex with Theophylline==
			<StructureSection load='3rox' size='340' side='right' caption='[[3rox]], [[Resolution\|resolution]] 2.40Å' scene=''>
			== Structural highlights ==
			<table><tr><td colspan='2'>[[3rox]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ROX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ROX FirstGlance]. <br>
			</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=TEP:THEOPHYLLINE'>TEP</scene></td></tr>
			<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
			<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2o8n\|2o8n]], [[2dg2\|2dg2]], [[3rno\|3rno]], [[3ro7\|3ro7]], [[3roe\|3roe]], [[3rog\|3rog]], [[3roz\|3roz]]</td></tr>
			<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">Aibp, Apoa1bp ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus])</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=3rox FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rox OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3rox RCSB], [http://www.ebi.ac.uk/pdbsum/3rox PDBsum]</span></td></tr>
			</table>
			<div style="background-color:#fffaf0;">
			== Publication Abstract from PubMed ==
			Proteins of unknown function comprise a significant fraction of sequenced genomes. Defining the roles of these proteins is vital to understanding cellular processes. Here, we describe a method to determine a protein function based on the identification of its natural ligand(s) by the crystallographic screening of the binding of a metabolite library, followed by a focused search in the metabolic space. The method was applied to two protein families with unknown function, PF01256 and YjeF_N. The PF01256 proteins, represented by YxkO from Bacillus subtilis and the C-terminal domain of Tm0922 from Thermotoga maritima, were shown to catalyze ADP/ATP-dependent NAD(P)H-hydrate dehydratation, a previously described orphan activity. The YjeF_N proteins, represented by mouse apolipoprotein A-I binding protein and the N-terminal domain of Tm0922, were found to interact with an adenosine diphosphoribose-related substrate and likely serve as ADP-ribosyltransferases. Crystallographic screening of metabolites serves as an efficient tool in functional analyses of uncharacterized proteins.

	~~{{STRUCTURE_3rox\| PDB=3rox \| SCENE= }}~~		Identification of Unknown Protein Function Using Metabolite Cocktail Screening.,Shumilin IA, Cymborowski M, Chertihin O, Jha KN, Herr JC, Lesley SA, Joachimiak A, Minor W Structure. 2012 Aug 28. PMID:22940582<ref>PMID:22940582</ref>

	~~===Crystal Structure~~ of ~~Mouse Apolipoprotein A-I Binding Protein in Complex with Theophylline===~~		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
			</div>
	~~{{ABSTRACT_PUBMED_22940582}}~~		== References ==
			<references/>
	==~~About this Structure~~==		__TOC__
	~~[[3rox]] is a 1 chain structure with sequence from [http:~~//~~en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ROX OCA].~~		</StructureSection>
	[[Category: Mus musculus]]		[[Category: Mus musculus]]
	[[Category: Cymborowski, M.]]		[[Category: Cymborowski, M]]
	[[Category: Herr, J C.]]		[[Category: Herr, J C]]
	[[Category: Jha, K N.]]		[[Category: Jha, K N]]
	[[Category: Minor, W.]]		[[Category: Minor, W]]
	[[Category: Shumilin, I A.]]		[[Category: Shumilin, I A]]
	[[Category: Protein binding]]		[[Category: Protein binding]]
	[[Category: Rossmann fold]]		[[Category: Rossmann fold]]

OCA at 09:02, 31 October 2012

2012-10-31T09:02:42Z

← Older revision		Revision as of 09:02, 31 October 2012
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	[[Image:3rox.~~jpg~~\|left\|200px]]		[[Image:3rox.png\|left\|200px]]

	{{STRUCTURE_3rox\| PDB=3rox \| SCENE= }}		{{STRUCTURE_3rox\| PDB=3rox \| SCENE= }}
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	===Crystal Structure of Mouse Apolipoprotein A-I Binding Protein in Complex with Theophylline===		===Crystal Structure of Mouse Apolipoprotein A-I Binding Protein in Complex with Theophylline===

			{{ABSTRACT_PUBMED_22940582}}

	==About this Structure==		==About this Structure==

OCA at 05:27, 18 July 2012

2012-07-18T05:27:20Z

← Older revision		Revision as of 05:27, 18 July 2012
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	~~'''Unreleased structure'''~~		[[Image:3rox.jpg\|left\|200px]]

	~~The entry~~ 3rox ~~is ON HOLD~~ ~~until Paper Publication~~		{{STRUCTURE_3rox\| PDB=3rox \| SCENE= }}

	~~Authors: Shumilin,~~ I~~.A., Jha, K.N., Cymborowski, M., Herr, J.C., Minor, W.~~		===Crystal Structure of Mouse Apolipoprotein A-I Binding Protein in Complex with Theophylline===

	~~Description~~: ~~Crystal Structure of Mouse Apolipoprotein A~~-I ~~Binding~~ Protein ~~in Complex with Theophylline~~
			==About this Structure==
			[[3rox]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ROX OCA].
			[[Category: Mus musculus]]
			[[Category: Cymborowski, M.]]
			[[Category: Herr, J C.]]
			[[Category: Jha, K N.]]
			[[Category: Minor, W.]]
			[[Category: Shumilin, I A.]]
			[[Category: Protein binding]]
			[[Category: Rossmann fold]]

OCA at 05:14, 18 May 2011

2011-05-18T05:14:20Z

← Older revision		Revision as of 05:14, 18 May 2011
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

	The entry 3rox is ON HOLD		The entry 3rox is ON HOLD until Paper Publication

	Authors: Shumilin, I.A., Jha, K.N., Cymborowski, M., Herr, J.C., Minor, W.		Authors: Shumilin, I.A., Jha, K.N., Cymborowski, M., Herr, J.C., Minor, W.

	Description: Crystal Structure of Mouse Apolipoprotein A-I Binding Protein in Complex with Theophylline		Description: Crystal Structure of Mouse Apolipoprotein A-I Binding Protein in Complex with Theophylline