1l5a
From Proteopedia
Crystal Structure of VibH, an NRPS Condensation Enzyme
Overview
Nonribosomal peptide synthetases (NRPSs) are large, multidomain enzymes that biosynthesize medically important natural products. We report the crystal structure of the free-standing NRPS condensation (C) domain VibH, which catalyzes amide bond formation in the synthesis of vibriobactin, a Vibrio cholerae siderophore. Despite low sequence identity, NRPS condensation enzymes are structurally related to chloramphenicol acetyltransferase (CAT) and dihydrolipoamide acyltransferases. However, although the latter enzymes are homotrimers, VibH is a monomeric pseudodimer. The VibH structure is representative of both NRPS condensation and epimerization domains, as well as the condensation-variant cyclization domains, which are all expected to be monomers. Surprisingly, despite favorable positioning in the active site, a universally conserved histidine important in CAT and in other C domains is not critical for general base catalysis in VibH.
About this Structure
1L5A is a Single protein structure of sequence from Vibrio cholerae. Full crystallographic information is available from OCA.
Reference
The structure of VibH represents nonribosomal peptide synthetase condensation, cyclization and epimerization domains., Keating TA, Marshall CG, Walsh CT, Keating AE, Nat Struct Biol. 2002 Jul;9(7):522-6. PMID:12055621 Page seeded by OCA on Fri May 2 23:33:12 2008
