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Lookup NU author(s): Professor Del Besra
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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 Å, reveals an α/β-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 Å 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.
Author(s): Running DR, Klabunde T, Besra GS, Vissa VD, Belisle JI, Sacchettini JC
Publication type: Article
Publication status: Published
Journal: Nature Structural Biology
ISSN (print): 1545-9993
Publisher: Nature Publishing Group
PubMed id: 10655617
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