1wa8: Difference between revisions
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==Solution Structure of the CFP-10.ESAT-6 Complex. Major Virulence Determinants of Pathogenic Mycobacteria== | |||
<StructureSection load='1wa8' size='340' side='right'caption='[[1wa8]]' scene=''> | |||
| | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1wa8]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis_H37Rv Mycobacterium tuberculosis H37Rv] and [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis_variant_bovis Mycobacterium tuberculosis variant bovis]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WA8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1WA8 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> | |||
| | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1wa8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wa8 OCA], [https://pdbe.org/1wa8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1wa8 RCSB], [https://www.ebi.ac.uk/pdbsum/1wa8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1wa8 ProSAT]</span></td></tr> | ||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/ESXB_MYCBO ESXB_MYCBO] A secreted protein. Acts as a strong host T-cell antigen. Involved in translocation of bacteria from the host (human) phagolysosome to the host cytoplasm. Might serve as a chaperone to prevent uncontrolled membrane lysis by its partner EsxA.[UniProtKB:P9WNK5] | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
== | Check<jmol> | ||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/wa/1wa8_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1wa8 ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
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. | 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. | ||
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<ref>PMID:15973432</ref> | |||
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 | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1wa8" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Mycobacterium tuberculosis H37Rv]] | |||
[[Category: Mycobacterium tuberculosis variant bovis]] | |||
[[Category: Burke B]] | |||
[[Category: Carr MD]] | |||
[[Category: Frenkiel TA]] | |||
[[Category: Gordon SV]] | |||
[[Category: Hewinson RG]] | |||
[[Category: Kelly G]] | |||
[[Category: Lightbody KL]] | |||
[[Category: Muskett FW]] | |||
[[Category: Norman J]] | |||
[[Category: Renshaw PS]] | |||
[[Category: Veverka V]] | |||
[[Category: Williamson RA]] | |||
Latest revision as of 13:33, 9 May 2024
Solution Structure of the CFP-10.ESAT-6 Complex. Major Virulence Determinants of Pathogenic Mycobacteria
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