2jgp

File:2jgp.gif

spinqualitylabelsall models 2jgp, resolution 1.85Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D

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 SO4, NA and DIO as ligands. Known structural/functional Sites: AC1, AC2, AC3, AC4 and AC5. 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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