2mlp
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(New page: 200px<br /><applet load="2mlp" size="450" color="white" frame="true" align="right" spinBox="true" caption="2mlp" /> '''MICROCIN LEADER PEPTIDE FROM E. COLI, NMR, 2...)
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Revision as of 10:38, 21 November 2007
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MICROCIN LEADER PEPTIDE FROM E. COLI, NMR, 25 STRUCTURES
Overview
BACKGROUND: The peptide antibiotic microcin B17 (MccB17) contains oxazole, and thiazole heterocycles formed by the post-translational modification of, four cysteine and four serine residues. An amino-terminal propeptide, targets the 69 amino acid precursor of MccB17 (preproMccB17) to the, heterocyclization enzyme MccB17 synthetase. The mode of synthetase, recognition has been unclear, because there has been limited structural, information available on the MccB17 propeptide to date. RESULTS: The, solution structure of the MccB17 propeptide (McbA1-26), determined using, nuclear magnetic resonance, reveals that McbA1-26 is an amphipathic alpha, helix. Mutational analysis of 13 propeptide residues showed that Phe8 and, Leu12 are essential residues for MccB17 synthetase recognition. A domain, of the propeptide was putatively identified as the region that interacts, with the synthetase. CONCLUSIONS: MccB17 synthetase recognizes key, hydrophobic residues within a helical propeptide, allowing the selective, heterocyclization of downstream cysteine and serine residues in, preproMccB17. The determination of the solution structure of the, propeptide should facilitate the investigation of other functions of the, propeptide, including a potential role in antibiotic secretion.
About this Structure
2MLP is a Single protein structure of sequence from Escherichia coli with NH2 as ligand. Full crystallographic information is available from OCA.
Reference
Role of the microcin B17 propeptide in substrate recognition: solution structure and mutational analysis of McbA1-26., Roy RS, Kim S, Baleja JD, Walsh CT, Chem Biol. 1998 Apr;5(4):217-28. PMID:9545435
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