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1WA8

Solution Structure of the CFP-10.ESAT-6 Complex. Major Virulence Determinants of Pathogenic Mycobacteria

Summary for 1WA8
Entry DOI10.2210/pdb1wa8/pdb
DescriptorESAT-6 LIKE PROTEIN ESXB, 6 KDA EARLY SECRETORY ANTIGENIC TARGET (ESAT-6) (2 entities in total)
Functional Keywordstuberculosis, cfp-10, esat-6, helix-turn-helix, four helix bundle, mycobacteria, pathogenesis, solution structure, psi, protein structure initiative, tb structural genomics consortium, tbsgc
Biological sourceMYCOBACTERIUM BOVIS
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Total number of polymer chains2
Total formula weight20580.35
Authors
Primary citationRenshaw, P.S.,Lightbody, K.L.,Veverka, V.,Muskett, F.W.,Kelly, G.,Frenkiel, T.A.,Gordon, S.V.,Hewinson, R.G.,Burke, B.,Norman, J.,Williamson, R.A.,Carr, M.D.
Structure and Function of the Complex Formed by the Tuberculosis Virulence Factors Cfp-10 and Esat-6
Embo J., 24:2491-, 2005
Cited by
PubMed Abstract: 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.
PubMed: 15973432
DOI: 10.1038/SJ.EMBOJ.7600732
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

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