1lmh
From Proteopedia
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Crystal Structure of S. aureus peptide deformylase
Overview
The first crystal structure of Class II peptide deformylase has been, determined. The enzyme from Staphylococcus aureus has been overexpressed, and purified in Escherichia coli and the structure determined by x-ray, crystallography to 1.9 A resolution. The purified iron-enriched form of S., aureus peptide deformylase enzyme retained high activity over many months., In contrast, the iron-enriched form of the E. coli enzyme is very labile., Comparison of the two structures details many differences; however, there, is no structural explanation for the dramatic activity differences we, observed. The protein structure of the S. aureus enzyme reveals a fold, similar, but not identical to, the well characterized E. coli enzyme. The, most striking deviation of the S. aureus from the E. coli structure is the, unique conformation of the C-terminal amino acids. The distinctive, C-terminal helix of the latter is replaced by a strand in S. aureus which, wraps around the enzyme, terminating near the active site. Although there, are no differences at the amino acid level near the active site metal ion, significant changes are noted in the peptide binding cleft which may play, a role in the design of general peptide deformylase inhibitors.
About this Structure
1LMH is a Single protein structure of sequence from Staphylococcus aureus with ZN as ligand. Active as N-formylmethionylaminoacyl-tRNA deformylase, with EC number 3.5.1.27 Full crystallographic information is available from OCA.
Reference
Crystal structure of type II peptide deformylase from Staphylococcus aureus., Baldwin ET, Harris MS, Yem AW, Wolfe CL, Vosters AF, Curry KA, Murray RW, Bock JH, Marshall VP, Cialdella JI, Merchant MH, Choi G, Deibel MR Jr, J Biol Chem. 2002 Aug 23;277(34):31163-71. Epub 2002 Jun 4. PMID:12048187
Page seeded by OCA on Tue Nov 20 20:40:41 2007
