The contribution of coevolving residues to the stability of KDO8P synthase.

ABSTRACT:

Background

The evolutionary tree of 3-deoxy-D-manno-octulosonate 8-phosphate (KDO8P) synthase (KDO8PS), a bacterial enzyme that catalyzes a key step in the biosynthesis of bacterial endotoxin, is evenly divided between metal and non-metal forms, both having similar structures, but diverging in various degrees in amino acid sequence. Mutagenesis, crystallographic and computational studies have established that only a few residues determine whether or not KDO8PS requires a metal for function. The remaining divergence in the amino acid sequence of KDO8PSs is apparently unrelated to the underlying catalytic mechanism.

Methodology/principal findings

The multiple alignment of all known KDO8PS sequences reveals that several residue pairs coevolved, an indication of their possible l

SUBMITTER: Ackerman SH 

PROVIDER: S-EPMC3052366 | biostudies-literature | 2011 Mar

REPOSITORIES: biostudies-literature