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| | <StructureSection load='6om4' size='340' side='right'caption='[[6om4]], [[Resolution|resolution]] 1.70Å' scene=''> | | <StructureSection load='6om4' size='340' side='right'caption='[[6om4]], [[Resolution|resolution]] 1.70Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6om4]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6OM4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6OM4 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6om4]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6OM4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6OM4 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=ND7:5-O-[(S)-amino(hydroxy)phosphoryl]adenosine'>ND7</scene>, <scene name='pdbligand=POP:PYROPHOSPHATE+2-'>POP</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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]] 1.7Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=FME:N-FORMYLMETHIONINE'>FME</scene></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FME:N-FORMYLMETHIONINE'>FME</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=ND7:[(2~{R},3~{S},4~{R},5~{R})-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methoxyphosphonamidic+acid'>ND7</scene>, <scene name='pdbligand=POP:PYROPHOSPHATE+2-'>POP</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">mccB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</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=6om4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6om4 OCA], [https://pdbe.org/6om4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6om4 RCSB], [https://www.ebi.ac.uk/pdbsum/6om4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6om4 ProSAT]</span></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=6om4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6om4 OCA], [http://pdbe.org/6om4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6om4 RCSB], [http://www.ebi.ac.uk/pdbsum/6om4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6om4 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/MCCC7_ECOLX MCCC7_ECOLX]] Antibacterial peptide, active against enterobacteria including species of Klebsiella, Salmonella, Shigella, Yersinia and Proteus, and strains of E.coli. Inhibits protein translation by blocking aspartyl-tRNA synthetase function and inhibiting production of aminoacetylated tRNA-Asp.<ref>PMID:2861788</ref> <ref>PMID:16574659</ref> <ref>PMID:18223070</ref> <ref>PMID:7559516</ref> <ref>PMID:17827970</ref> <ref>PMID:17711420</ref> | + | [https://www.uniprot.org/uniprot/Q47506_ECOLX Q47506_ECOLX] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacillus coli migula 1895]] | + | [[Category: Escherichia coli]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Dong, S H]] | + | [[Category: Dong S-H]] |
| - | [[Category: Nair, S K]] | + | [[Category: Nair SK]] |
| - | [[Category: Biosynthetic protein]]
| + | |
| - | [[Category: Microcin c7]]
| + | |
| - | [[Category: Phosphoramidate]]
| + | |
| - | [[Category: Trojan horse antibiotic]]
| + | |
| Structural highlights
6om4 is a 4 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Method: | X-ray diffraction, Resolution 1.7Å |
| Ligands: | , , , , |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
Q47506_ECOLX
Publication Abstract from PubMed
Microcin C7 (McC) is a peptide antibiotic modified by a linkage of the terminal isoAsn amide to AMP via a phosphoramidate bond. Post-translational modification on this ribosomally produced heptapeptide precursor is carried out by MccB, which consumes two equivalents of ATP to generate the N-P linkage. We demonstrate that MccB only efficiently processes the precursor heptapeptide that retains the N-formylated initiator Met (fMet). Binding studies and kinetic measurements evidence the role of the N-formyl moiety. Structural data show that the N-formyl peptide binding results in an ordering of residues in the MccB "crossover loop", which dictates specificity in homologous ubiquitin activating enzymes. The N-formyl peptide exhibits substrate inhibition, and cannot be displaced from MccB by the desformyl counterpart. Such substrate inhibition may be a strategy to avert unwanted McC buildup and avert toxicity in the cytoplasm of producing organisms.
Biosynthesis of the RiPP trojan horse nucleotide antibiotic microcin C is directed by the N-formyl of the peptide precursor.,Dong SH, Kulikovsky A, Zukher I, Estrada P, Dubiley S, Severinov K, Nair SK Chem Sci. 2018 Dec 26;10(8):2391-2395. doi: 10.1039/c8sc03173h. eCollection 2019 , Feb 28. PMID:30881667[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Dong SH, Kulikovsky A, Zukher I, Estrada P, Dubiley S, Severinov K, Nair SK. Biosynthesis of the RiPP trojan horse nucleotide antibiotic microcin C is directed by the N-formyl of the peptide precursor. Chem Sci. 2018 Dec 26;10(8):2391-2395. doi: 10.1039/c8sc03173h. eCollection 2019 , Feb 28. PMID:30881667 doi:http://dx.doi.org/10.1039/c8sc03173h
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