2jgp

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spinqualitylabelsall models 2jgp, resolution 1.85Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

STRUCTURE OF THE TYCC5-6 PCP-C BIDOMAIN OF THE TYROCIDINE SYNTHETASE TYCC

Overview

The crystal structure of the bidomain PCP-C from modules 5 and 6 of the, nonribosomal tyrocidine synthetase TycC was determined at 1.8 A, resolution. The bidomain structure reveals a V-shaped condensation domain, the canyon-like active site groove of which is associated with the, preceding peptidyl carrier protein (PCP) domain at its donor side. The, relative arrangement of the PCP and the peptide bond-forming condensation, (C) domain places the active sites approximately 50 A apart. Accordingly, this PCP-C structure represents a conformational state prior to peptide, transfer from the donor-PCP to the acceptor-PCP domain, implying the, existence of additional states of PCP-C domain interaction during, catalysis. Additionally, PCP-C exerts a mode of cyclization activity that, mimics peptide bond formation catalyzed by C domains. Based on mutational, data and pK value analysis of active site residues, it is suggested that, nonribosomal peptide bond formation depends on electrostatic interactions, rather than on general acid/base catalysis.

About this Structure

2JGP is a Single protein structure of sequence from Brevibacillus brevis with , and as ligands. Known structural/functional Sites: , , , and . Full crystallographic information is available from OCA.

Reference

Structural and functional insights into a peptide bond-forming bidomain from a nonribosomal peptide synthetase., Samel SA, Schoenafinger G, Knappe TA, Marahiel MA, Essen LO, Structure. 2007 Jul;15(7):781-92. PMID:17637339

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