4yx7: Difference between revisions
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==Complex of SpaO(SPOA1,2) and OrgB(APAR)::T4lysozyme fusion protein== | ==Complex of SpaO(SPOA1,2) and OrgB(APAR)::T4lysozyme fusion protein== | ||
<StructureSection load='4yx7' size='340' side='right' caption='[[4yx7]], [[Resolution|resolution]] 2.00Å' scene=''> | <StructureSection load='4yx7' size='340' side='right'caption='[[4yx7]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4yx7]] is a 6 chain structure with sequence from [ | <table><tr><td colspan='2'>[[4yx7]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_virus_T4 Escherichia virus T4] and [https://en.wikipedia.org/wiki/Salmonella_enterica_subsp._enterica_serovar_Typhimurium_str._LT2 Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4YX7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4YX7 FirstGlance]. <br> | ||
</td></tr> | </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=4yx7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4yx7 OCA], [https://pdbe.org/4yx7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4yx7 RCSB], [https://www.ebi.ac.uk/pdbsum/4yx7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4yx7 ProSAT]</span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/SPAO_SALTY SPAO_SALTY] Involved in a secretory pathway responsible for the surface presentation of determinants needed for the entry of Salmonella species into mammalian cells. | ||
<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: | [[Category: Escherichia virus T4]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]] | ||
[[Category: Notti | [[Category: Notti RQ]] | ||
[[Category: Stebbins | [[Category: Stebbins CE]] | ||
Revision as of 10:29, 10 May 2023
Complex of SpaO(SPOA1,2) and OrgB(APAR)::T4lysozyme fusion proteinComplex of SpaO(SPOA1,2) and OrgB(APAR)::T4lysozyme fusion protein
Structural highlights
FunctionSPAO_SALTY Involved in a secretory pathway responsible for the surface presentation of determinants needed for the entry of Salmonella species into mammalian cells. Publication Abstract from PubMedTranslocating proteins across the double membrane of Gram-negative bacteria, type III secretion systems (T3SS) occur in two evolutionarily related forms: injectisomes, delivering virulence factors into host cells, and the flagellar system, secreting the polymeric filament used for motility. While both systems share related elements of a cytoplasmic sorting platform that facilitates the hierarchical secretion of protein substrates, its assembly and regulation remain unclear. Here we describe a module mediating the assembly of the sorting platform in both secretion systems, and elucidate the structural basis for segregation of homologous components among these divergent T3SS subtypes sharing a common cytoplasmic milieu. These results provide a foundation for the subtype-specific assembly of T3SS sorting platforms and will support further mechanistic analysis and anti-virulence drug design. A common assembly module in injectisome and flagellar type III secretion sorting platforms.,Notti RQ, Bhattacharya S, Lilic M, Stebbins CE Nat Commun. 2015 May 21;6:7125. doi: 10.1038/ncomms8125. PMID:25994170[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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