5yhh: Difference between revisions
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<StructureSection load='5yhh' size='340' side='right'caption='[[5yhh]], [[Resolution|resolution]] 2.00Å' scene=''> | <StructureSection load='5yhh' size='340' side='right'caption='[[5yhh]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5yhh]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5YHH OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[5yhh]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Geobacillus_stearothermophilus Geobacillus stearothermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5YHH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5YHH 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]] 2Å</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=OCS:CYSTEINESULFONIC+ACID'>OCS</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=5yhh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5yhh OCA], [https://pdbe.org/5yhh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5yhh RCSB], [https://www.ebi.ac.uk/pdbsum/5yhh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5yhh ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/A0A150NEL9_GEOSE A0A150NEL9_GEOSE] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Geobacillus stearothermophilus]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Kim | [[Category: Kim JH]] | ||
[[Category: Namgung | [[Category: Namgung B]] | ||
[[Category: Song | [[Category: Song WS]] | ||
[[Category: Yoon | [[Category: Yoon SI]] | ||
Latest revision as of 11:30, 22 November 2023
Crystal structure of YiiM from Geobacillus stearothermophilusCrystal structure of YiiM from Geobacillus stearothermophilus
Structural highlights
FunctionPublication Abstract from PubMedThe molybdenum cofactor (Moco) is a molybdenum-conjugated prosthetic group that is ubiquitously found in plants, animals, and bacteria. Moco is required for the nitrogen-reducing reaction of the Moco sulfurase C-terminal domain (MOSC) family. Despite the biological significance of MOSC proteins in the conversion of prodrugs and resistance against mutagens, their structural features and Moco-mediated catalysis mechanism have not been described in detail. YiiM is a MOSC protein that is involved in reducing mutagenic 6-N-hydroxylaminopurine to nontoxic adenine in bacteria. Here, we report two crystal structures of YiiM: one from Gram-positive Geobacillus stearothermophilus (gsYiiM) and the other from Gram-negative Escherichia coli (ecYiiM). Although gsYiiM and ecYiiM differ in oligomerization state and protein stability, both consist of three structural modules (a beta-barrel and two alpha-helix bundles) and feature a cavity surrounded by the three modules. The cavity is characterized by positive electrostatic potentials and high sequence conservation. Moreover, the ecYiiM cavity houses a phosphate group, which emulates a part of Moco, and contains a highly reactive invariant cysteine residue. We thus propose that the cavity is the catalytic site where Moco binds and the substrate is reduced. Moreover, our comparative structural analysis highlights the common but distinct structural features of MOSC proteins. Crystal structure of the hydroxylaminopurine resistance protein, YiiM, and its putative molybdenum cofactor-binding catalytic site.,Namgung B, Kim JH, Song WS, Yoon SI Sci Rep. 2018 Feb 19;8(1):3304. doi: 10.1038/s41598-018-21660-y. PMID:29459651[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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