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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 Adenosine-3'-5'-Diphosphate==
==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 Adenosine-3'-5'-Diphosphate==
<StructureSection load='3rtb' size='340' side='right' caption='[[3rtb]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
<StructureSection load='3rtb' size='340' side='right'caption='[[3rtb]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3rtb]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_43589 Atcc 43589] and [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3RTB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3RTB FirstGlance]. <br>
<table><tr><td colspan='2'>[[3rtb]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_BL21(DE3) Escherichia coli BL21(DE3)] and [https://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3RTB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3RTB FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=A3P:ADENOSINE-3-5-DIPHOSPHATE'>A3P</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</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]] 2.1&#8491;</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]], [[3rtc|3rtc]], [[3rtd|3rtd]], [[3rte|3rte]], [[3rtg|3rtg]], [[3ru2|3ru2]], [[3ru3|3ru3]]</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=A3P:ADENOSINE-3-5-DIPHOSPHATE'>A3P</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene></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=2336 ATCC 43589])</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=3rtb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rtb OCA], [https://pdbe.org/3rtb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3rtb RCSB], [https://www.ebi.ac.uk/pdbsum/3rtb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3rtb 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/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=3rtb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rtb OCA], [http://pdbe.org/3rtb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3rtb RCSB], [http://www.ebi.ac.uk/pdbsum/3rtb PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3rtb ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[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).  
[https://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;">
== 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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3rtb" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Atcc 43589]]
[[Category: Large Structures]]
[[Category: Escherichia coli]]
[[Category: Thermotoga maritima]]
[[Category: Cymborowski, M]]
[[Category: Cymborowski M]]
[[Category: Lesley, S A]]
[[Category: Lesley SA]]
[[Category: Minor, W]]
[[Category: Minor W]]
[[Category: Shumilin, I A]]
[[Category: Shumilin IA]]
[[Category: Lyase]]
[[Category: Unknown function]]

Latest revision as of 15:36, 14 March 2024

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 Adenosine-3'-5'-DiphosphateCrystal 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 Adenosine-3'-5'-Diphosphate

Structural highlights

3rtb is a 2 chain structure with sequence from Escherichia coli BL21(DE3) and Thermotoga maritima. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.1Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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).

3rtb, resolution 2.10Å

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