6p2t
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==BshB from Bacillus subtilis complexed with citrate== | |
| + | <StructureSection load='6p2t' size='340' side='right'caption='[[6p2t]], [[Resolution|resolution]] 1.85Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6p2t]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6P2T OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6P2T FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=6p2t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6p2t OCA], [http://pdbe.org/6p2t PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6p2t RCSB], [http://www.ebi.ac.uk/pdbsum/6p2t PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6p2t ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/BSHB1_BACSU BSHB1_BACSU]] Involved in bacillithiol (BSH) biosynthesis. Catalyzes the second step of the pathway, the deacetylation of N-acetylglucosaminylmalate (GlcNAc-Mal) to glucosamine malate (GlcN-Mal).[UniProtKB:Q81ST8] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Many gram-positive bacteria produce bacillithiol to aid in the maintenance of redox homeostasis and degradation of toxic compounds, including the antibiotic fosfomycin. Bacillithiol is produced via a three-enzyme pathway that includes the action of the zinc-dependent deacetylase BshB. Previous studies identified conserved aspartate and histidine residues within the active site that are involved in metal binding and catalysis, but the enzymatic mechanism is not fully understood. Here we report two X-ray crystallographic structures of BshB from Bacillus subtilis that provide insight into the BshB catalytic mechanism. | ||
| - | + | X-ray crystallographic structure of BshB, the zinc-dependent deacetylase involved in bacillithiol biosynthesis.,Woodward RL, Castleman MM, Meloche CE, Karpen ME, Carlson CG, Yobi WH, Jepsen JC, Lewis BW, Zarnosky BN, Cook PD Protein Sci. 2019 Dec 22. doi: 10.1002/pro.3808. PMID:31867856<ref>PMID:31867856</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: Cook, P | + | <div class="pdbe-citations 6p2t" style="background-color:#fffaf0;"></div> |
| - | [[Category: Meloche, C | + | == References == |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Cook, P D]] | ||
| + | [[Category: Meloche, C E]] | ||
| + | [[Category: Bacillithiol]] | ||
| + | [[Category: Deacetylase]] | ||
| + | [[Category: Hydrolase]] | ||
| + | [[Category: Metal-dependent]] | ||
Revision as of 07:36, 8 January 2020
BshB from Bacillus subtilis complexed with citrate
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