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==Structure and features of the complex formed by the tuberculosis virulence factors Rv0287 and Rv0288==
==Structure and features of the complex formed by the tuberculosis virulence factors Rv0287 and Rv0288==
<StructureSection load='2kg7' size='340' side='right' caption='[[2kg7]], [[NMR_Ensembles_of_Models | 30 NMR models]]' scene=''>
<StructureSection load='2kg7' size='340' side='right'caption='[[2kg7]]' scene=''>
== Structural highlights ==
== Structural highlights ==
[[2kg7]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KG7 OCA]. <br>
<table><tr><td colspan='2'>[[2kg7]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis_H37Rv Mycobacterium tuberculosis H37Rv]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KG7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2KG7 FirstGlance]. <br>
<b>Activity:</b> <span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span><br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
<b>Resources:</b> <span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2kg7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2kg7 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2kg7 RCSB], [http://www.ebi.ac.uk/pdbsum/2kg7 PDBsum]</span><br>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2kg7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2kg7 OCA], [https://pdbe.org/2kg7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2kg7 RCSB], [https://www.ebi.ac.uk/pdbsum/2kg7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2kg7 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/ESXG_MYCTU ESXG_MYCTU] EsxG, in complex with EsxH, disrupts ESCRT function and impairs host phagosome maturation, thereby promoting intracellular bacterial growth. The complex acts by interacting, via EsxH, with the host hepatocyte growth factor-regulated tyrosine kinase substrate (HGS/HRS), a component of the ESCRT machinery. EsxG stabilizes EsxH in the host cytosol.<ref>PMID:24204276</ref>  
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/kg/2kg7_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/kg/2kg7_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
   </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/chain_selection.php?pdb_ID=2ata ConSurf].
</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=2kg7 ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
== References ==
== References ==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Mycobacterium tuberculosis]]
[[Category: Large Structures]]
[[Category: Carr, M D.]]
[[Category: Mycobacterium tuberculosis H37Rv]]
[[Category: Ilghari, D.]]
[[Category: Carr MD]]
[[Category: Kirsty, L L.]]
[[Category: Ilghari D]]
[[Category: Philip, R S.]]
[[Category: Kirsty LL]]
[[Category: Veverka, V L.]]
[[Category: Philip RS]]
[[Category: Waters, L C.]]
[[Category: Veverka VL]]
[[Category: Protein complex]]
[[Category: Waters LC]]
[[Category: Unknown function]]

Latest revision as of 09:45, 1 May 2024

Structure and features of the complex formed by the tuberculosis virulence factors Rv0287 and Rv0288Structure and features of the complex formed by the tuberculosis virulence factors Rv0287 and Rv0288

Structural highlights

2kg7 is a 2 chain structure with sequence from Mycobacterium tuberculosis H37Rv. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Solution NMR
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

ESXG_MYCTU EsxG, in complex with EsxH, disrupts ESCRT function and impairs host phagosome maturation, thereby promoting intracellular bacterial growth. The complex acts by interacting, via EsxH, with the host hepatocyte growth factor-regulated tyrosine kinase substrate (HGS/HRS), a component of the ESCRT machinery. EsxG stabilizes EsxH in the host cytosol.[1]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

References

  1. ↑ Mehra A, Zahra A, Thompson V, Sirisaengtaksin N, Wells A, Porto M, Köster S, Penberthy K, Kubota Y, Dricot A, Rogan D, Vidal M, Hill DE, Bean AJ, Philips JA. Mycobacterium tuberculosis type VII secreted effector EsxH targets host ESCRT to impair trafficking. PLoS Pathog. 2013 Oct;9(10):e1003734. PMID:24204276 doi:10.1371/journal.ppat.1003734
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