1LMH

Crystal Structure of S. aureus peptide deformylase

Summary for 1LMH

• Entry DOI: 10.2210/pdb1lmh/pdb
• Descriptor: PROTEIN (S.aureus peptide deformylase), ZINC ION (3 entities in total)
• Functional Keywords: zinc peptidase, hydrolase
• Biological source: Staphylococcus aureus
• Total number of polymer chains: 1
• Total formula weight: 21046.47

Authors

Baldwin, E.T.,Harris, M.S. (deposition date: 2002-05-01, release date: 2002-06-12, Last modification date: 2024-10-30)

Primary citation

Baldwin, E.T.,Harris, M.S.,Yem, A.W.,Wolfe, C.L.,Vosters, A.F.,Curry, K.A.,Murray, R.W.,Bock, J.H.,Marshall, V.P.,Cialdella, J.I.,Merchant, M.H.,Choi, G.,Deibel Jr., M.R.
Crystal Structure of Type II peptide deformylase from Staphylococcus aureus
J.Biol.Chem., 277:31163-31171, 2002

PubMed Abstract: 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.

PubMed: 12048187
DOI: 10.1074/jbc.M202750200

Experimental method

X-RAY DIFFRACTION (1.9 Å)