2aie: Difference between revisions

Revision as of 19:44, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2aie.png

Template:STRUCTURE 2aie

S.pneumoniae polypeptide deformylase complexed with SB-505684S.pneumoniae polypeptide deformylase complexed with SB-505684

Template:ABSTRACT PUBMED 12538898

About this StructureAbout this Structure

2AIE is a Single protein structure of sequence from Streptococcus pneumoniae. Full crystallographic information is available from OCA.

ReferenceReference

Structural variation and inhibitor binding in polypeptide deformylase from four different bacterial species., Smith KJ, Petit CM, Aubart K, Smyth M, McManus E, Jones J, Fosberry A, Lewis C, Lonetto M, Christensen SB, Protein Sci. 2003 Feb;12(2):349-60. PMID:12538898

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OCA

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-'''S.pneumoniae polypeptide deformylase complexed with SB-505684'''
+===S.pneumoniae polypeptide deformylase complexed with SB-505684===
-==Overview==
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-Polypeptide deformylase (PDF) catalyzes the deformylation of polypeptide chains in bacteria. It is essential for bacterial cell viability and is a potential antibacterial drug target. Here, we report the crystal structures of polypeptide deformylase from four different species of bacteria: Streptococcus pneumoniae, Staphylococcus aureus, Haemophilus influenzae, and Escherichia coli. Comparison of these four structures reveals significant overall differences between the two Gram-negative species (E. coli and H. influenzae) and the two Gram-positive species (S. pneumoniae and S. aureus). Despite these differences and low overall sequence identity, the S1' pocket of PDF is well conserved among the four enzymes studied. We also describe the binding of nonpeptidic inhibitor molecules SB-485345, SB-543668, and SB-505684 to both S. pneumoniae and E. coli PDF. Comparison of these structures shows similar binding interactions with both Gram-negative and Gram-positive species. Understanding the similarities and subtle differences in active site structure between species will help to design broad-spectrum polypeptide deformylase inhibitor molecules.
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 [[Category: Smyth, M.]]
 [[Category: Hydrolase]]
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