Structures of a Nonribosomal Peptide Synthetase Module Bound to MbtH-like Proteins Support a Highly Dynamic Domain Architecture
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منابع مشابه
Crystal structure of the termination module of a nonribosomal peptide synthetase.
Nonribosomal peptide synthetases (NRPSs) are modular multidomain enzymes that act as an assembly line to catalyze the biosynthesis of complex natural products. The crystal structure of the 144-kilodalton Bacillus subtilis termination module SrfA-C was solved at 2.6 angstrom resolution. The adenylation and condensation domains of SrfA-C associate closely to form a catalytic platform, with their ...
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Nonribosomal peptide synthetases responsible for the production of macrocyclic compounds often use their C-terminal thioesterase (TE) domain for enzymatic cyclization of a linear precursor. The excised TE domain from the nonribosomal peptide synthetase responsible for the production of the cyclic decapeptide tyrocidine A, TycC TE, retains autonomous ability to catalyze head-to-tail macrocycliza...
متن کاملEpsilon-poly-L-lysine dispersity is controlled by a highly unusual nonribosomal peptide synthetase.
Epsilon-Poly-L-lysine (epsilon-PL) consists of 25-35 L-lysine residues in isopeptide linkages and is one of only two amino acid homopolymers known in nature. Elucidating the biosynthetic mechanism of epsilon-PL should open new avenues for creating novel classes of biopolymers. Here we report the purification of an epsilon-PL synthetase (Pls; 130 kDa) and the cloning of its gene from an epsilon-...
متن کاملe-Poly-L-lysine dispersity is controlled by a highly unusual nonribosomal peptide synthetase
e-Poly-L-lysine (e-PL) consists of 25–35 L-lysine residues in isopeptide linkages and is one of only two amino acid homopolymers known in nature. Elucidating the biosynthetic mechanism of e-PL should open new avenues for creating novel classes of biopolymers. Here we report the purification of an e-PL synthetase (Pls; 130 kDa) and the cloning of its gene from an e-PL–producing strain of Strepto...
متن کاملThe crystal structure of BlmI as a model for nonribosomal peptide synthetase peptidyl carrier proteins.
Carrier proteins (CPs) play a critical role in the biosynthesis of various natural products, especially in nonribosomal peptide synthetase (NRPS) and polyketide synthase (PKS) enzymology, where the CPs are referred to as peptidyl-carrier proteins (PCPs) or acyl-carrier proteins (ACPs), respectively. CPs can either be a domain in large multifunctional polypeptides or standalone proteins, termed ...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 2016
ISSN: 0021-9258
DOI: 10.1074/jbc.m116.746297