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| | <StructureSection load='5lhk' size='340' side='right'caption='[[5lhk]], [[Resolution|resolution]] 2.32Å' scene=''> | | <StructureSection load='5lhk' size='340' side='right'caption='[[5lhk]], [[Resolution|resolution]] 2.32Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5lhk]] is a 1 chain structure with sequence from [http://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 [http://proteopedia.org/fgij/fg.htm?mol=5LHK FirstGlance]. <br> | + | <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='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> | + | </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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">botP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1109705 Streptomyces sp. BC16019])</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'>[http://proteopedia.org/fgij/fg.htm?mol=5lhk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lhk OCA], [http://pdbe.org/5lhk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5lhk RCSB], [http://www.ebi.ac.uk/pdbsum/5lhk PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5lhk ProSAT]</span></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> | | </table> |
| | == Function == | | == Function == |
| - | [[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] | + | [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;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Streptomyces sp. bc16019]] | + | [[Category: Streptomyces sp. BC16019]] |
| - | [[Category: Adam, S]] | + | [[Category: Adam S]] |
| - | [[Category: Koehnke, J]] | + | [[Category: Koehnke J]] |
| - | [[Category: Botp]]
| + | |
| - | [[Category: Bottromycin]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Peptidase]]
| + | |
| - | [[Category: Ripp]]
| + | |
| Structural highlights
Function
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]
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Mann G, Huo L, Adam S, Nardone B, Vendome J, Westwood NJ, Muller R, Koehnke J. Structure and substrate recognition of the Bottromycin maturation enzyme BotP. Chembiochem. 2016 Sep 21. doi: 10.1002/cbic.201600406. PMID:27653442 doi:http://dx.doi.org/10.1002/cbic.201600406
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