1e6c: Difference between revisions
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Revision as of 16:02, 30 October 2007
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K15M MUTANT OF SHIKIMATE KINASE FROM ERWINIA CHRYSANTHEMI
OverviewOverview
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 ... [(full description)]
About this StructureAbout this Structure
1E6C is a [Single protein] structure of sequence from [Erwinia chrysanthemi] with PO4, CL, MRD and MPD as [ligands]. Active as [Shikimate kinase], with EC number [2.7.1.71]. Structure known Active Sites: POA and POB. Full crystallographic information is available from [OCA].
ReferenceReference
Biochemical and X-ray crystallographic studies on shikimate kinase: the important structural role of the P-loop lysine., Krell T, Maclean J, Boam DJ, Cooper A, Resmini M, Brocklehurst K, Kelly SM, Price NC, Lapthorn AJ, Coggins JR, Protein Sci. 2001 Jun;10(6):1137-49. PMID:11369852
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