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==Crystal structure of tm0922, a fusion of a domain of unknown function and ADP/ATP-dependent NAD(P)H-hydrate dehydratase from Thermotoga maritima soaked with NADPH and ATP.== | ==Crystal structure of tm0922, a fusion of a domain of unknown function and ADP/ATP-dependent NAD(P)H-hydrate dehydratase from Thermotoga maritima soaked with NADPH and ATP.== | ||
<StructureSection load='3ru3' size='340' side='right' caption='[[3ru3]], [[Resolution|resolution]] 2.60Å' scene=''> | <StructureSection load='3ru3' size='340' side='right' caption='[[3ru3]], [[Resolution|resolution]] 2.60Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3ru3]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] and [http://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[3ru3]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] and [http://en.wikipedia.org/wiki/Thema Thema]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3RU3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3RU3 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NDP:NADPH+DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NDP</scene>, <scene name='pdbligand=NPW:BETA-6-HYDROXY-1,4,5,6-TETRAHYDRONICOTINAMIDE+ADENINE+DINUCLEOTIDE+PHOSPHATE'>NPW</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NDP:NADPH+DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NDP</scene>, <scene name='pdbligand=NPW:BETA-6-HYDROXY-1,4,5,6-TETRAHYDRONICOTINAMIDE+ADENINE+DINUCLEOTIDE+PHOSPHATE'>NPW</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2ax3|2ax3]], [[3rno|3rno]], [[3ro7|3ro7]], [[3roe|3roe]], [[3rog|3rog]], [[3rox|3rox]], [[3roz|3roz]], [[3rrb|3rrb]], [[3rre|3rre]], [[3rrf|3rrf]], [[3rrj|3rrj]], [[3rs8|3rs8]], [[3rs9|3rs9]], [[3rsf|3rsf]], [[3rsg|3rsg]], [[3rsq|3rsq]], [[3rss|3rss]], [[3rt7|3rt7]], [[3rt9|3rt9]], [[3rta|3rta]], [[3rtb|3rtb]], [[3rtc|3rtc]], [[3rtd|3rtd]], [[3rte|3rte]], [[3rtg|3rtg]], [[3ru2|3ru2]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2ax3|2ax3]], [[3rno|3rno]], [[3ro7|3ro7]], [[3roe|3roe]], [[3rog|3rog]], [[3rox|3rox]], [[3roz|3roz]], [[3rrb|3rrb]], [[3rre|3rre]], [[3rrf|3rrf]], [[3rrj|3rrj]], [[3rs8|3rs8]], [[3rs9|3rs9]], [[3rsf|3rsf]], [[3rsg|3rsg]], [[3rsq|3rsq]], [[3rss|3rss]], [[3rt7|3rt7]], [[3rt9|3rt9]], [[3rta|3rta]], [[3rtb|3rtb]], [[3rtc|3rtc]], [[3rtd|3rtd]], [[3rte|3rte]], [[3rtg|3rtg]], [[3ru2|3ru2]]</td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">tm0922, TM_0922 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=243274 | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">tm0922, TM_0922 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=243274 THEMA])</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/ATP-dependent_NAD(P)H-hydrate_dehydratase ATP-dependent NAD(P)H-hydrate dehydratase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.93 4.2.1.93] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/ATP-dependent_NAD(P)H-hydrate_dehydratase ATP-dependent NAD(P)H-hydrate dehydratase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.93 4.2.1.93] </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=3ru3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ru3 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3ru3 RCSB], [http://www.ebi.ac.uk/pdbsum/3ru3 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=3ru3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ru3 OCA], [http://pdbe.org/3ru3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3ru3 RCSB], [http://www.ebi.ac.uk/pdbsum/3ru3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3ru3 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/ | [[http://www.uniprot.org/uniprot/NNR_THEMA NNR_THEMA]] Bifunctional enzyme that catalyzes the epimerization of the S- and R-forms of NAD(P)HX and the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. This allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration (By similarity). | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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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 3ru3" style="background-color:#fffaf0;"></div> | |||
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: | [[Category: Thema]] | ||
[[Category: Cymborowski, M]] | [[Category: Cymborowski, M]] | ||
[[Category: Lesley, S A]] | [[Category: Lesley, S A]] | ||
Revision as of 10:20, 4 August 2016
Crystal structure of tm0922, a fusion of a domain of unknown function and ADP/ATP-dependent NAD(P)H-hydrate dehydratase from Thermotoga maritima soaked with NADPH and ATP.Crystal structure of tm0922, a fusion of a domain of unknown function and ADP/ATP-dependent NAD(P)H-hydrate dehydratase from Thermotoga maritima soaked with NADPH and ATP.
Structural highlights
Function[NNR_THEMA] Bifunctional enzyme that catalyzes the epimerization of the S- and R-forms of NAD(P)HX and the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. This allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration (By similarity). Publication Abstract from PubMedProteins 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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