4yxa: Difference between revisions
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''' | ==Complex of SpaO(SPOA1,2 SeMet) and OrgB(APAR)::T4lysozyme fusion protein== | ||
<StructureSection load='4yxa' size='340' side='right' caption='[[4yxa]], [[Resolution|resolution]] 2.35Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4yxa]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4YXA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4YXA FirstGlance]. <br> | |||
</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | |||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Lysozyme Lysozyme], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.17 3.2.1.17] </span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4yxa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4yxa OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4yxa RCSB], [http://www.ebi.ac.uk/pdbsum/4yxa PDBsum]</span></td></tr> | |||
</table> | |||
== Function == | |||
[[http://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. [[http://www.uniprot.org/uniprot/ORGB_SALTY ORGB_SALTY]] Oxygen-regulated protein required for bacterial internalization. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Translocating 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<ref>PMID:25994170</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
[[Category: | <references/> | ||
[[Category: Stebbins, C | __TOC__ | ||
[[Category: | </StructureSection> | ||
[[Category: Lysozyme]] | |||
[[Category: Notti, R Q]] | |||
[[Category: Stebbins, C E]] | |||
[[Category: Protein transport]] | |||
[[Category: Type iii secretion system]] |