1L5A

Crystal Structure of VibH, an NRPS Condensation Enzyme

Summary for 1L5A

• Entry DOI: 10.2210/pdb1l5a/pdb
• Descriptor: amide synthase (2 entities in total)
• Functional Keywords: nonribosomal peptide synthetase, nrps condensation domain, amide synthase, vibriobactin, biosynthetic protein
• Biological source: Vibrio cholerae
• Total number of polymer chains: 3
• Total formula weight: 149385.22

Authors

Keating, T.A.,Marshall, C.G.,Walsh, C.T.,Keating, A.E. (deposition date: 2002-03-06, release date: 2002-06-26, Last modification date: 2024-02-14)

Primary citation

Keating, T.A.,Marshall, C.G.,Walsh, C.T.,Keating, A.E.
The structure of VibH represents nonribosomal peptide synthetase condensation, cyclization and epimerization domains.
Nat.Struct.Biol., 9:522-526, 2002

PubMed Abstract: 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.

PubMed: 12055621

Experimental method

X-RAY DIFFRACTION (2.55 Å)