2mlp | pdb_00002mlp

MICROCIN LEADER PEPTIDE FROM E. COLI, NMR, 25 STRUCTURES

spinqualitylabelsall models 2mlp, 25 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2mlp is a 1 chain structure with sequence from Escherichia coli. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. NonStd Res: NH2 Resources: FirstGlance, OCA, RCSB, PDBsum Publication Abstract from PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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