2ca5: Difference between revisions
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< | ==MxiH needle protein of Shigella Flexneri (monomeric form, residues 1- 78)== | ||
<StructureSection load='2ca5' size='340' side='right'caption='[[2ca5]], [[Resolution|resolution]] 2.10Å' scene=''> | |||
You may | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2ca5]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Shigella_flexneri Shigella flexneri]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CA5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2CA5 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1Å</td></tr> | |||
- | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=IPA:ISOPROPYL+ALCOHOL'>IPA</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></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=2ca5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ca5 OCA], [https://pdbe.org/2ca5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ca5 RCSB], [https://www.ebi.ac.uk/pdbsum/2ca5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ca5 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/MXIH_SHIFL MXIH_SHIFL] Necessary for the secretion of IPA invasins. | |||
== 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/ca/2ca5_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=2ca5 ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Type III secretion systems are essential virulence determinants for many Gram-negative bacterial pathogens. The type III secretion system consists of cytoplasmic, transmembrane, and extracellular domains. The extracellular domain is a hollow needle protruding above the bacterial surface and is held within a basal body that traverses both bacterial membranes. Effector proteins are translocated, via this external needle, directly into host cells, where they subvert normal cell functions to aid infection. Physical contact with host cells initiates secretion and leads to formation of a pore, thought to be contiguous with the needle channel, in the host-cell membrane. Here, we report the crystal structure of the Shigella flexneri needle subunit MxiH and a complete model for the needle assembly built into our three-dimensional EM reconstruction. The model, combined with mutagenesis data, reveals that signaling of host-cell contact is relayed through the needle via intersubunit contacts and suggests a mode of binding for a tip complex. | |||
Molecular model of a type III secretion system needle: Implications for host-cell sensing.,Deane JE, Roversi P, Cordes FS, Johnson S, Kenjale R, Daniell S, Booy F, Picking WD, Picking WL, Blocker AJ, Lea SM Proc Natl Acad Sci U S A. 2006 Aug 15;103(33):12529-33. Epub 2006 Aug 3. PMID:16888041<ref>PMID:16888041</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2ca5" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | [[Category: Large Structures]] | ||
== | |||
< | |||
[[Category: Shigella flexneri]] | [[Category: Shigella flexneri]] | ||
[[Category: Blocker | [[Category: Blocker AJ]] | ||
[[Category: Cordes | [[Category: Cordes FS]] | ||
[[Category: Deane | [[Category: Deane JE]] | ||
[[Category: Johnson | [[Category: Johnson S]] | ||
[[Category: Kenjale | [[Category: Kenjale R]] | ||
[[Category: Lea | [[Category: Lea SM]] | ||
[[Category: Picking | [[Category: Picking WD]] | ||
[[Category: Picking | [[Category: Picking WL]] | ||
[[Category: Roversi | [[Category: Roversi P]] | ||
Latest revision as of 12:23, 9 May 2024
MxiH needle protein of Shigella Flexneri (monomeric form, residues 1- 78)MxiH needle protein of Shigella Flexneri (monomeric form, residues 1- 78)
Structural highlights
FunctionMXIH_SHIFL Necessary for the secretion of IPA invasins. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedType III secretion systems are essential virulence determinants for many Gram-negative bacterial pathogens. The type III secretion system consists of cytoplasmic, transmembrane, and extracellular domains. The extracellular domain is a hollow needle protruding above the bacterial surface and is held within a basal body that traverses both bacterial membranes. Effector proteins are translocated, via this external needle, directly into host cells, where they subvert normal cell functions to aid infection. Physical contact with host cells initiates secretion and leads to formation of a pore, thought to be contiguous with the needle channel, in the host-cell membrane. Here, we report the crystal structure of the Shigella flexneri needle subunit MxiH and a complete model for the needle assembly built into our three-dimensional EM reconstruction. The model, combined with mutagenesis data, reveals that signaling of host-cell contact is relayed through the needle via intersubunit contacts and suggests a mode of binding for a tip complex. Molecular model of a type III secretion system needle: Implications for host-cell sensing.,Deane JE, Roversi P, Cordes FS, Johnson S, Kenjale R, Daniell S, Booy F, Picking WD, Picking WL, Blocker AJ, Lea SM Proc Natl Acad Sci U S A. 2006 Aug 15;103(33):12529-33. Epub 2006 Aug 3. PMID:16888041[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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