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5lhj

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m (Protected "5lhj" [edit=sysop:move=sysop])
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'''Unreleased structure'''
 
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The entry 5lhj is ON HOLD
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==Bottromycin maturation enzyme BotP==
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<StructureSection load='5lhj' size='340' side='right' caption='[[5lhj]], [[Resolution|resolution]] 1.76&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[5lhj]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LHJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5LHJ 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=1PE:PENTAETHYLENE+GLYCOL'>1PE</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></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=5lhj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lhj OCA], [http://pdbe.org/5lhj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5lhj RCSB], [http://www.ebi.ac.uk/pdbsum/5lhj PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5lhj ProSAT]</span></td></tr>
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</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/K4MHW2_9ACTN K4MHW2_9ACTN]] Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides.[SAAS:SAAS00610869]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The bottromycins are a family of highly modified peptide natural products displaying potent antimicrobial activity against Gram-positive bacteria including methicillin-resistant Staphyloccoccus aureus. Bottromycins have recently been shown to be ribosomally synthesized and post-translationally modified peptides (RiPPs). Uniquely amongst RiPPs the precursor peptide BotA contains a C-terminal follower, rather than the canonical N- terminal leader sequence. We report the structural and biochemical characterization of BotP, a leucyl-aminopeptidase like enzyme from the bottromycin pathway. We demonstrate that BotP is responsible for the removal of the N-terminal methionine from the precursor peptide. The crystal structures of apo BotP and of BotP in complex with Mn2+ allowed us to model a BotP/substrate complex and to rationalize substrate recognition. Our data represent the first step towards targeted compound modification to unlock the full antibiotic potential of bottromycin.
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Authors:
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Structure and substrate recognition of the Bottromycin maturation enzyme BotP.,Mann G, Huo L, Adam S, Nardone B, Vendome J, Westwood NJ, Muller R, Koehnke J Chembiochem. 2016 Sep 21. doi: 10.1002/cbic.201600406. PMID:27653442<ref>PMID:27653442</ref>
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Description:
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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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<div class="pdbe-citations 5lhj" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Koehnke, J]]
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[[Category: Mann, G]]
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[[Category: Botp]]
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[[Category: Bottromycin]]
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[[Category: Hydrolase]]
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[[Category: Ripp]]

Revision as of 17:45, 19 October 2016

Bottromycin maturation enzyme BotP

5lhj, resolution 1.76Å

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