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| | <StructureSection load='2jlj' size='340' side='right'caption='[[2jlj]], [[Resolution|resolution]] 1.30Å' scene=''> | | <StructureSection load='2jlj' size='340' side='right'caption='[[2jlj]], [[Resolution|resolution]] 1.30Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2jlj]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_pestis"_(lehmann_and_neumann_1896)_migula_1900 "bacillus pestis" (lehmann and neumann 1896) migula 1900]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JLJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2JLJ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2jlj]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Yersinia_pestis Yersinia pestis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JLJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2JLJ FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2jli|2jli]], [[2jlh|2jlh]]</div></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]] 1.3Å</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=2jlj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jlj OCA], [https://pdbe.org/2jlj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2jlj RCSB], [https://www.ebi.ac.uk/pdbsum/2jlj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2jlj 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=2jlj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jlj OCA], [https://pdbe.org/2jlj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2jlj RCSB], [https://www.ebi.ac.uk/pdbsum/2jlj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2jlj ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/YSCU_YERPE YSCU_YERPE]] Component of the yop secretion machinery (By similarity).
| + | [https://www.uniprot.org/uniprot/YSCU_YERPE YSCU_YERPE] Component of the yop secretion machinery (By similarity). |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Austin, B P]] | + | [[Category: Yersinia pestis]] |
| - | [[Category: Lountos, G T]] | + | [[Category: Austin BP]] |
| - | [[Category: Nallamsetty, S]] | + | [[Category: Lountos GT]] |
| - | [[Category: Waugh, D S]] | + | [[Category: Nallamsetty S]] |
| - | [[Category: Cell membrane]] | + | [[Category: Waugh DS]] |
| - | [[Category: Membrane]]
| + | |
| - | [[Category: Protein transport]]
| + | |
| - | [[Category: Transmembrane]]
| + | |
| - | [[Category: Transport]]
| + | |
| - | [[Category: Type iii secretion system]]
| + | |
| - | [[Category: Virulence]]
| + | |
| - | [[Category: Yersinia pesit]]
| + | |
| Structural highlights
Function
YSCU_YERPE Component of the yop secretion machinery (By similarity).
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 PubMed
Crystal structures of cleaved and uncleaved forms of the YscU cytoplasmic domain, an essential component of the type III secretion system (T3SS) in Yersinia pestis, have been solved by single-wavelength anomolous dispersion and refined with X-ray diffraction data extending up to atomic resolution (1.13 A). These crystallographic studies provide structural insights into the conformational changes induced upon auto-cleavage of the cytoplasmic domain of YscU. The structures indicate that the cleaved fragments remain bound to each other. The conserved NPTH sequence that contains the site of the N263-P264 peptide bond cleavage is found on a beta-turn which, upon cleavage, undergoes a major reorientation of the loop away from the catalytic N263, resulting in altered electrostatic surface features at the site of cleavage. Additionally, a significant conformational change was observed in the N-terminal linker regions of the cleaved and noncleaved forms of YscU which may correspond to the molecular switch that influences substrate specificity. The YscU structures determined here also are in good agreement with the auto-cleavage mechanism described for the flagellar homolog FlhB and E. coli EscU.
Atomic resolution structure of the cytoplasmic domain of Yersinia pestis YscU, a regulatory switch involved in type III secretion.,Lountos GT, Austin BP, Nallamsetty S, Waugh DS Protein Sci. 2009 Jan 6;18(2):467-474. PMID:19165725[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Lountos GT, Austin BP, Nallamsetty S, Waugh DS. Atomic resolution structure of the cytoplasmic domain of Yersinia pestis YscU, a regulatory switch involved in type III secretion. Protein Sci. 2009 Jan 6;18(2):467-474. PMID:19165725 doi:10.1002/pro.56
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