Structure of PA1221, a nonribosomal peptide synthetase containing adenylation and peptidyl carrier protein domains.

ABSTRACT: Many bacteria use large modular enzymes for the synthesis of polyketide and peptide natural products. These multidomain enzymes contain integrated carrier domains that deliver bound substrates to multiple catalytic domains, requiring coordination of these chemical steps. Nonribosomal peptide synthetases (NRPSs) load amino acids onto carrier domains through the activity of an upstream adenylation domain. Our lab recently determined the structure of an engineered two-domain NRPS containing fused adenylation and carrier domains. This structure adopted a domain-swapped dimer that illustrated the interface between these two domains. To continue our investigation, we now examine PA1221, a natural two-domain protein from Pseudomonas aeruginosa. We have determined the amino acid specificity of thi

SUBMITTER: Mitchell CA 

PROVIDER: S-EPMC3332334 | biostudies-literature | 2012 Apr

REPOSITORIES: biostudies-literature