4yxc: Difference between revisions

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-'''Unreleased structure'''
+==Complex of FliM(SPOA)::FliN fusion protein and FliH(APAR)::T4lysozyme fusion protein==
+<StructureSection load='4yxc' size='340' side='right' caption='[[4yxc]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[4yxc]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4YXC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4YXC FirstGlance]. <br>
+</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=4yxc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4yxc OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4yxc RCSB], [http://www.ebi.ac.uk/pdbsum/4yxc PDBsum]</span></td></tr>
+</table>
+== Function ==
+[[http://www.uniprot.org/uniprot/FLIM_SALTY FLIM_SALTY]] FliM is one of three proteins (FliG, FliN, FliM) that forms the rotor-mounted switch complex (C ring), located at the base of the basal body. This complex interacts with the CheY and CheZ chemotaxis proteins, in addition to contacting components of the motor that determine the direction of flagellar rotation (By similarity).
+<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.
-The entry 4yxc is ON HOLD  until Paper Publication
+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>
-Authors: Notti, R.Q., Stebbins, C.E.
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
-Description:
+== References ==
-[[Category: Unreleased Structures]]
+<references/>
-[[Category: Stebbins, C.E]]
+__TOC__
-[[Category: Notti, R.Q]]
+</StructureSection>
+[[Category: Lysozyme]]
+[[Category: Notti, R Q]]
+[[Category: Stebbins, C E]]
+[[Category: Protein transport]]
+[[Category: Type iii secretion system]]