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Nat Struct Biol. 2000 Feb;7(2):141-6.

Crystal structure of the secreted form of antigen 85C reveals potential targets for mycobacterial drugs and vaccines.

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1
Department of Biochemistry and Biophysics, Texas A&M University, College Station, Texas 77844-2128, USA.

Abstract

The antigen 85 (ag85) complex, composed of three proteins (ag85A, B and C), is a major protein component of the Mycobacterium tuberculosis cell wall. Each protein possesses a mycolyltransferase activity required for the biogenesis of trehalose dimycolate (cord factor), a dominant structure necessary for maintaining cell wall integrity. The crystal structure of recombinant ag85C from M. tuberculosis, refined to a resolution of 1.5 A, reveals an alpha/beta-hydrolase polypeptide fold, and a catalytic triad formed by Ser 124, Glu 228 and His 260. ag85C complexed with a covalent inhibitor implicates residues Leu 40 and Met 125 as components of the oxyanion hole. A hydrophobic pocket and tunnel extending 21 A into the core of the protein indicates the location of a probable trehalose monomycolate binding site. Also, a large region of conserved surface residues among ag85A, B and C is a probable site for the interaction of ag85 proteins with human fibronectin.

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PMID:
10655617
DOI:
10.1038/72413
[Indexed for MEDLINE]

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