1wa8

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SOLUTION STRUCTURE OF THE CFP-10.ESAT-6 COMPLEX. MAJOR VIRULENCE DETERMINANTS OF PATHOGENIC MYCOBACTERIA

Overview

The secreted Mycobacterium tuberculosis complex proteins CFP-10 and ESAT-6, have recently been shown to play an essential role in tuberculosis, pathogenesis. We have determined the solution structure of the tight, 1:1, complex formed by CFP-10 and ESAT-6, and employed fluorescence microscopy, to demonstrate specific binding of the complex to the surface of, macrophage and monocyte cells. A striking feature of the complex is the, long flexible arm formed by the C-terminus of CFP-10, which was found to, be essential for binding to the surface of cells. The surface features of, the CFP-10.ESAT-6 complex, together with observed binding to specific host, cells, strongly suggest a key signalling role for the complex, in which, binding to cell surface receptors leads to modulation of host cell, behaviour to the advantage of the pathogen.

About this Structure

1WA8 is a Protein complex structure of sequences from Mycobacterium bovis and Mycobacterium tuberculosis. Full crystallographic information is available from OCA.

Reference

Structure and function of the complex formed by the tuberculosis virulence factors CFP-10 and ESAT-6., Renshaw PS, Lightbody KL, Veverka V, Muskett FW, Kelly G, Frenkiel TA, Gordon SV, Hewinson RG, Burke B, Norman J, Williamson RA, Carr MD, EMBO J. 2005 Jul 20;24(14):2491-8. Epub 2005 Jun 23. PMID:15973432

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