Biochemical and X-ray crystallographic studies on shikimate kinase: the important structural role of the P-loop lysine.

ABSTRACT: Shikimate kinase, despite low sequence identity, has been shown to be structurally a member of the nucleoside monophosphate (NMP) kinase family, which includes adenylate kinase. In this paper we have explored the roles of residues in the P-loop of shikimate kinase, which forms the binding site for nucleotides and is one of the most conserved structural features in proteins. In common with many members of the P-loop family, shikimate kinase contains a cysteine residue 2 amino acids upstream of the essential lysine residue; the side chains of these residues are shown to form an ion pair. The C13S mutant of shikimate kinase was found to be enzymatically active, whereas the K15M mutant was inactive. However, the latter mutant had both increased thermostability and affinity for ATP when compare

SUBMITTER: Krell T 

PROVIDER: S-EPMC2374015 | biostudies-literature | 2001 Jun

REPOSITORIES: biostudies-literature