6ull

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'''Unreleased structure'''
 
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The entry 6ull is ON HOLD until Paper Publication
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==BshB from Bacillus subtilis complexed with a substrate analogue==
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<StructureSection load='6ull' size='340' side='right'caption='[[6ull]], [[Resolution|resolution]] 1.45&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[6ull]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6ULL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6ULL FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=RWI:(2S)-2-({2-deoxy-2-[(hydroxycarbamoyl)amino]-alpha-D-glucopyranosyl}oxy)butanedioic+acid'>RWI</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6p2t|6p2t]]</td></tr>
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<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=6ull FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ull OCA], [http://pdbe.org/6ull PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ull RCSB], [http://www.ebi.ac.uk/pdbsum/6ull PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ull ProSAT]</span></td></tr>
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</table>
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== Function ==
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[[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]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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Authors: Cook, P.D., Castleman, M.M., Woodward, R.L.
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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>
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Description: BshB from Bacillus subtilis complexed with a substrate analogue
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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[[Category: Woodward, R.L]]
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<div class="pdbe-citations 6ull" style="background-color:#fffaf0;"></div>
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[[Category: Cook, P.D]]
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== References ==
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[[Category: Castleman, M.M]]
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Castleman, M M]]
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[[Category: Cook, P D]]
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[[Category: Woodward, R L]]
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[[Category: Bacillithiol]]
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[[Category: Deacetylase]]
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[[Category: Gram-positive]]
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[[Category: Hydrolase]]
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[[Category: Hydroxamic acid]]

Revision as of 07:42, 8 January 2020

BshB from Bacillus subtilis complexed with a substrate analogue

PDB ID 6ull

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