5imy: Difference between revisions

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<StructureSection load='5imy' size='340' side='right'caption='[[5imy]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
<StructureSection load='5imy' size='340' side='right'caption='[[5imy]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[5imy]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/"corynebacterium_vaginale"_zinnemann_and_turner_1963 "corynebacterium vaginale" zinnemann and turner 1963] and [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5IMY OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5IMY FirstGlance]. <br>
<table><tr><td colspan='2'>[[5imy]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Gardnerella_vaginalis Gardnerella vaginalis] and [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5IMY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5IMY FirstGlance]. <br>
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">VLY, vly ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2702 "Corynebacterium vaginale" Zinnemann and Turner 1963]), CD59, MIC11, MIN1, MIN2, MIN3, MSK21 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5imy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5imy OCA], [http://pdbe.org/5imy PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5imy RCSB], [http://www.ebi.ac.uk/pdbsum/5imy PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5imy ProSAT]</span></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=5imy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5imy OCA], [https://pdbe.org/5imy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5imy RCSB], [https://www.ebi.ac.uk/pdbsum/5imy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5imy ProSAT]</span></td></tr>
</table>
</table>
== Disease ==
[[http://www.uniprot.org/uniprot/CD59_HUMAN CD59_HUMAN]] Defects in CD59 are the cause of CD59 deficiency (CD59D) [MIM:[http://omim.org/entry/612300 612300]].<ref>PMID:1382994</ref> 
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/CD59_HUMAN CD59_HUMAN]] Potent inhibitor of the complement membrane attack complex (MAC) action. Acts by binding to the C8 and/or C9 complements of the assembling MAC, thereby preventing incorporation of the multiple copies of C9 required for complete formation of the osmolytic pore. This inhibitor appears to be species-specific. Involved in signal transduction for T-cell activation complexed to a protein tyrosine kinase.  The soluble form from urine retains its specific complement binding activity, but exhibits greatly reduced ability to inhibit MAC assembly on cell membranes.
[https://www.uniprot.org/uniprot/B2YGA4_GARVA B2YGA4_GARVA]  
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Corynebacterium vaginale zinnemann and turner 1963]]
[[Category: Gardnerella vaginalis]]
[[Category: Human]]
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Lawrence, S L]]
[[Category: Lawrence SL]]
[[Category: Morton, C J]]
[[Category: Morton CJ]]
[[Category: Parker, M W]]
[[Category: Parker MW]]
[[Category: Toxin-toxin receptor complex]]

Latest revision as of 17:02, 30 August 2023

Trapped ToxinTrapped Toxin

Structural highlights

5imy is a 4 chain structure with sequence from Gardnerella vaginalis and Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.4Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

B2YGA4_GARVA

Publication Abstract from PubMed

Cholesterol-dependent cytolysins (CDCs) are a family of pore-forming toxins that punch holes in the outer membrane of eukaryotic cells. Cholesterol serves as the receptor, but a subclass of CDCs first binds to human CD59. Here we describe the crystal structures of vaginolysin and intermedilysin complexed to CD59. These studies, together with small-angle X-ray scattering, reveal that CD59 binds to each at different, though overlapping, sites, consistent with molecular dynamics simulations and binding studies. The CDC consensus undecapeptide motif, which for the CD59-responsive CDCs has a proline instead of a tryptophan in the motif, adopts a strikingly different conformation between the structures; our data suggest that the proline acts as a selectivity switch to ensure CD59-dependent CDCs bind their protein receptor first in preference to cholesterol. The structural data suggest a detailed model of how these water-soluble toxins assemble as prepores on the cell surface.

Structural Basis for Receptor Recognition by the Human CD59-Responsive Cholesterol-Dependent Cytolysins.,Lawrence SL, Gorman MA, Feil SC, Mulhern TD, Kuiper MJ, Ratner AJ, Tweten RK, Morton CJ, Parker MW Structure. 2016 Sep 6;24(9):1488-1498. doi: 10.1016/j.str.2016.06.017. Epub 2016 , Aug 4. PMID:27499440[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. Lawrence SL, Gorman MA, Feil SC, Mulhern TD, Kuiper MJ, Ratner AJ, Tweten RK, Morton CJ, Parker MW. Structural Basis for Receptor Recognition by the Human CD59-Responsive Cholesterol-Dependent Cytolysins. Structure. 2016 Sep 6;24(9):1488-1498. doi: 10.1016/j.str.2016.06.017. Epub 2016 , Aug 4. PMID:27499440 doi:http://dx.doi.org/10.1016/j.str.2016.06.017

5imy, resolution 2.40Å

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