1kyh: Difference between revisions
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<StructureSection load='1kyh' size='340' side='right'caption='[[1kyh]], [[Resolution|resolution]] 1.60Å' scene=''> | <StructureSection load='1kyh' size='340' side='right'caption='[[1kyh]], [[Resolution|resolution]] 1.60Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1kyh]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[1kyh]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KYH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KYH FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1kyh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kyh OCA], [https://pdbe.org/1kyh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1kyh RCSB], [https://www.ebi.ac.uk/pdbsum/1kyh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1kyh ProSAT], [https://www.topsan.org/Proteins/MCSG/1kyh TOPSAN]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/NNRD_BACSU NNRD_BACSU] Catalyzes the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. Together with NAD(P)HX epimerase, which catalyzes the epimerization of the S- and R-forms, the enzyme 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.[HAMAP-Rule:MF_01965] | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ky/1kyh_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ky/1kyh_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/ | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </jmolCheckbox> | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Bacillus | [[Category: Bacillus subtilis]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Collart | [[Category: Collart F]] | ||
[[Category: Dementieva | [[Category: Dementieva I]] | ||
[[Category: Joachimiak | [[Category: Joachimiak A]] | ||
[[Category: Vinokour E]] | |||
[[Category: Vinokour | [[Category: Zhang R]] | ||
[[Category: Zhang | |||
Latest revision as of 09:55, 30 October 2024
Structure of Bacillus subtilis YxkO, a Member of the UPF0031 Family and a Putative KinaseStructure of Bacillus subtilis YxkO, a Member of the UPF0031 Family and a Putative Kinase
Structural highlights
FunctionNNRD_BACSU Catalyzes the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. Together with NAD(P)HX epimerase, which catalyzes the epimerization of the S- and R-forms, the enzyme 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.[HAMAP-Rule:MF_01965] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedWe determined the 1.6-A resolution crystal structure of a conserved hypothetical 29.9-kDa protein from the SIGY-CYDD intergenic region encoded by a Bacillus subtilis open reading frame in the YXKO locus. YXKO homologues are broadly distributed and are by and large described as proteins with unknown function. The YXKO protein has an alpha/beta fold and shows high structural homology to the members of a ribokinase-like superfamily. However, YXKO is the only member of this superfamily known to form tetramers. Putative binding sites for adenosine triphosphate (ATP), a substrate, and Mg(2+)-binding sites were revealed in the structure of the protein, based on high structural similarity to ATP-dependent members of the superfamily. Two adjacent monomers contribute residues to the active site. The crystal structure provides valuable information about the YXKO protein's tertiary and quaternary structure, the biochemical function of YXKO and its homologues, and the evolution of its ribokinase-like superfamily. Structure of Bacillus subtilis YXKO--a member of the UPF0031 family and a putative kinase.,Zhang RG, Grembecka J, Vinokour E, Collart F, Dementieva I, Minor W, Joachimiak A J Struct Biol. 2002 Sep;139(3):161-70. PMID:12457846[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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