5lhk
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Bottromycin maturation enzyme BotP in complex with Mn== | |
| + | <StructureSection load='5lhk' size='340' side='right'caption='[[5lhk]], [[Resolution|resolution]] 2.32Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5lhk]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_sp._BC16019 Streptomyces sp. BC16019]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LHK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5LHK FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.32Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BCT:BICARBONATE+ION'>BCT</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</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=5lhk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lhk OCA], [https://pdbe.org/5lhk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5lhk RCSB], [https://www.ebi.ac.uk/pdbsum/5lhk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5lhk ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://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] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | 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. | ||
| - | + | 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> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 5lhk" style="background-color:#fffaf0;"></div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[Aminopeptidase 3D structures|Aminopeptidase 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Streptomyces sp. BC16019]] | ||
| + | [[Category: Adam S]] | ||
| + | [[Category: Koehnke J]] | ||
Current revision
Bottromycin maturation enzyme BotP in complex with Mn
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