1WA8
Solution Structure of the CFP-10.ESAT-6 Complex. Major Virulence Determinants of Pathogenic Mycobacteria
Summary for 1WA8
| Entry DOI | 10.2210/pdb1wa8/pdb |
| Descriptor | ESAT-6 LIKE PROTEIN ESXB, 6 KDA EARLY SECRETORY ANTIGENIC TARGET (ESAT-6) (2 entities in total) |
| Functional Keywords | tuberculosis, cfp-10, esat-6, helix-turn-helix, four helix bundle, mycobacteria, pathogenesis, solution structure, psi, protein structure initiative, tb structural genomics consortium, tbsgc |
| Biological source | MYCOBACTERIUM BOVIS More |
| Total number of polymer chains | 2 |
| Total formula weight | 20580.35 |
| Authors | Renshaw, 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.,TB Structural Genomics Consortium (TBSGC) (deposition date: 2004-10-25, release date: 2005-06-27, Last modification date: 2024-05-15) |
| Primary citation | Renshaw, 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: 15973432DOI: 10.1038/SJ.EMBOJ.7600732 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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