1l5a

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{{STRUCTURE_1l5a| PDB=1l5a | SCENE= }}
{{STRUCTURE_1l5a| PDB=1l5a | SCENE= }}
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'''Crystal Structure of VibH, an NRPS Condensation Enzyme'''
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===Crystal Structure of VibH, an NRPS Condensation Enzyme===
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==Overview==
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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.
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==About this Structure==
==About this Structure==
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[[Category: Nrps condensation domain]]
[[Category: Nrps condensation domain]]
[[Category: Vibriobactin]]
[[Category: Vibriobactin]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 11:43:57 2008''

Revision as of 08:44, 2 July 2008

Image:1l5a.png

Template:STRUCTURE 1l5a

Crystal Structure of VibH, an NRPS Condensation Enzyme

Template:ABSTRACT PUBMED 12055621

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

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