1ry9

<table><tr><td colspan='2'>[[1ry9]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/"shigella_paradysenteriae"_weldin_1927 "shigella paradysenteriae" weldin 1927]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RY9 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1RY9 FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SPAK, SPA15, CP0148 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=623 "Shigella paradysenteriae" Weldin 1927])</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=1ry9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ry9 OCA], [http://pdbe.org/1ry9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ry9 RCSB], [http://www.ebi.ac.uk/pdbsum/1ry9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1ry9 ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/SPAK_SHIFL SPAK_SHIFL]] Required for surface presentation of invasion plasmid antigens. Chaperone specialized in the storage of effectors within the bacterial cytoplasm, maintaining them in a secretion-competent state, and allowing their immediate delivery to target cells upon contact of the bacterium with the host cells. Has been shown to chaperone IpaA, IpgB1, OspC3 and probably also OspB.

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== Publication Abstract from PubMed ==

Type III secretion (TTS) systems are used by many Gram-negative pathogens to inject virulence proteins into the cells of their hosts. Several of these virulence effectors require TTS chaperones that maintain them in a secretion-competent state. Whereas most chaperones bind only one effector, Spa15 from the human pathogen Shigella flexneri and homologous chaperones bind several seemingly unrelated effectors, and were proposed to form a special subgroup. Its 1.8 A crystal structure confirms this specific classification, showing that Spa15 has the same fold as other TTS effector chaperones, but forms a different dimer. The presence of hydrophobic sites on the Spa15 surface suggests that the different Spa15 effectors all possess similar structural elements that can bind these sites. Furthermore, the Spa15 structure reveals larger structural differences between class I chaperones than previously anticipated, which does not support the hypothesis that chaperone-effector complexes are structurally conserved and function as three-dimensional secretion signals.

Structure of Spa15, a type III secretion chaperone from Shigella flexneri with broad specificity.,van Eerde A, Hamiaux C, Perez J, Parsot C, Dijkstra BW EMBO Rep. 2004 May;5(5):477-83. Epub 2004 Apr 16. PMID:15088068<ref>PMID:15088068</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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== References ==

<references/>

[[Category: Shigella paradysenteriae weldin 1927]]

[[Category: Dijkstra, B W]]

[[Category: Eerde, A van]]

[[Category: Hamiaux, C]]

[[Category: Parsot, C]]

[[Category: Perez, J]]

[[Category: Alpha/beta fold]]

[[Category: Chaperone]]