3h9g

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[[Image:3h9g.png|left|200px]]
 
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{{STRUCTURE_3h9g| PDB=3h9g | SCENE= }}
{{STRUCTURE_3h9g| PDB=3h9g | SCENE= }}
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===Crystal structure of E. coli MccB + MccA-N7isoASN===
===Crystal structure of E. coli MccB + MccA-N7isoASN===
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{{ABSTRACT_PUBMED_19494832}}
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==Function==
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[[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>
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{{ABSTRACT_PUBMED_19494832}}
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==About this Structure==
==About this Structure==
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==Reference==
==Reference==
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<ref group="xtra">PMID:019494832</ref><references group="xtra"/>
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<ref group="xtra">PMID:019494832</ref><references group="xtra"/><references/>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Miller, D.]]
[[Category: Miller, D.]]

Revision as of 14:13, 10 July 2013

Template:STRUCTURE 3h9g

Contents

Crystal structure of E. coli MccB + MccA-N7isoASN

Template:ABSTRACT PUBMED 19494832

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]

About this Structure

3h9g is a 8 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

  • 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. ↑ 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
  2. ↑ 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
  3. ↑ 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
  4. ↑ 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
  5. ↑ 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
  6. ↑ 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

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