1DQZ

CRYSTAL STRUCTURE OF ANTIGEN 85C FROM MYCOBACTERIUM TUBERCULOSIS

Summary for 1DQZ

• Entry DOI: 10.2210/pdb1dqz/pdb
• Related: 1DQY
• Descriptor: PROTEIN (ANTIGEN 85-C) (2 entities in total)
• Functional Keywords: antigen, 85c, mycobacterium tuberculosis, fibronectin, structural genomics, psi, protein structure initiative, tb structural genomics consortium, tbsgc, immune system
• Biological source: Mycobacterium tuberculosis
• Cellular location: Secreted: P0A4V4
• Total number of polymer chains: 2
• Total formula weight: 61698.25

Authors

Ronning, D.R.,Klabunde, T.,Sacchettini, J.C.,TB Structural Genomics Consortium (TBSGC) (deposition date: 2000-01-05, release date: 2000-07-12, Last modification date: 2024-02-07)

Primary citation

Ronning, D.R.,Klabunde, T.,Besra, G.S.,Vissa, V.D.,Belisle, J.T.,Sacchettini, J.C.
Crystal structure of the secreted form of antigen 85C reveals potential targets for mycobacterial drugs and vaccines.
Nat.Struct.Biol., 7:141-146, 2000

PubMed 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.

PubMed: 10655617
DOI: 10.1038/72413

Experimental method

X-RAY DIFFRACTION (1.5 Å)