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3h9j

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Revision as of 21:07, 24 December 2014

Crystal structure of E. coli MccB + AMPCPP + SeMeT MccA

Structural highlights

3h9j is a 8 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, ,
NonStd Res:
Related:	3h5a, 3h5n, 3h5r, 3h9g, 3h9q
Gene:	mccB (Escherichia coli)
Resources:	FirstGlance, OCA, RCSB, PDBsum

Function

[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.^[1] ^[2] ^[3] ^[4] ^[5] ^[6]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

The 39-kDa Escherichia coli enzyme MccB catalyses a remarkable posttranslational modification of the MccA heptapeptide during the biosynthesis of microcin C7 (MccC7), a 'Trojan horse' antibiotic. The approximately 260-residue C-terminal region of MccB is homologous to ubiquitin-like protein (UBL) activating enzyme (E1) adenylation domains. Accordingly, MccB-catalysed C-terminal MccA-acyl-adenylation is reminiscent of the E1-catalysed activation reaction. However, unlike E1 substrates, which are UBLs with a C-terminal di-glycine sequence, MccB's substrate, MccA, is a short peptide with an essential C-terminal Asn. Furthermore, after an intramolecular rearrangement of MccA-acyl-adenylate, MccB catalyses a second, unique reaction, producing a stable phosphoramidate-linked analogue of acyl-adenylated aspartic acid. We report six-crystal structures of MccB in apo, substrate-, intermediate-, and inhibitor-bound forms. Structural and kinetic analyses reveal a novel-peptide clamping mechanism for MccB binding to heptapeptide substrates and a dynamic-active site for catalysing dual adenosine triphosphate-consuming reactions. The results provide insight into how a distinctive member of the E1 superfamily carries out two-step activation for generating the peptidyl-antibiotic MccC7.

How the MccB bacterial ancestor of ubiquitin E1 initiates biosynthesis of the microcin C7 antibiotic.,Regni CA, Roush RF, Miller DJ, Nourse A, Walsh CT, Schulman BA EMBO J. 2009 Jul 8;28(13):1953-64. Epub 2009 Jun 4. PMID:19494832^[7]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Garcia-Bustos JF, Pezzi N, Mendez E. Structure and mode of action of microcin 7, an antibacterial peptide produced by Escherichia coli. Antimicrob Agents Chemother. 1985 May;27(5):791-7. PMID:2861788
↑ Metlitskaya A, Kazakov T, Kommer A, Pavlova O, Praetorius-Ibba M, Ibba M, Krasheninnikov I, Kolb V, Khmel I, Severinov K. Aspartyl-tRNA synthetase is the target of peptide nucleotide antibiotic Microcin C. J Biol Chem. 2006 Jun 30;281(26):18033-42. Epub 2006 Mar 30. PMID:16574659 doi:10.1074/jbc.M513174200
↑ Kazakov T, Vondenhoff GH, Datsenko KA, Novikova M, Metlitskaya A, Wanner BL, Severinov K. Escherichia coli peptidase A, B, or N can process translation inhibitor microcin C. J Bacteriol. 2008 Apr;190(7):2607-10. doi: 10.1128/JB.01956-07. Epub 2008 Jan 25. PMID:18223070 doi:10.1128/JB.01956-07
↑ Guijarro JI, Gonzalez-Pastor JE, Baleux F, San Millan JL, Castilla MA, Rico M, Moreno F, Delepierre M. Chemical structure and translation inhibition studies of the antibiotic microcin C7. J Biol Chem. 1995 Oct 6;270(40):23520-32. PMID:7559516
↑ Duquesne S, Petit V, Peduzzi J, Rebuffat S. Structural and functional diversity of microcins, gene-encoded antibacterial peptides from enterobacteria. J Mol Microbiol Biotechnol. 2007;13(4):200-9. PMID:17827970 doi:10.1159/000104748
↑ Severinov K, Semenova E, Kazakov A, Kazakov T, Gelfand MS. Low-molecular-weight post-translationally modified microcins. Mol Microbiol. 2007 Sep;65(6):1380-94. Epub 2007 Aug 17. PMID:17711420 doi:10.1111/j.1365-2958.2007.05874.x
↑ Regni CA, Roush RF, Miller DJ, Nourse A, Walsh CT, Schulman BA. How the MccB bacterial ancestor of ubiquitin E1 initiates biosynthesis of the microcin C7 antibiotic. EMBO J. 2009 Jul 8;28(13):1953-64. Epub 2009 Jun 4. PMID:19494832 doi:10.1038/emboj.2009.146

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3h9j"

@@ Line 9: / Line 9: @@
 <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=3h9j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3h9j OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3h9j RCSB], [http://www.ebi.ac.uk/pdbsum/3h9j PDBsum]</span></td></tr>
 </table>
+== 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>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

3h9j

From Proteopedia

Revision as of 21:07, 24 December 2014

Crystal structure of E. coli MccB + AMPCPP + SeMeT MccA

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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