3ph0

<StructureSection load='3ph0' size='340' side='right' caption='[[3ph0]], [[Resolution|resolution]] 2.40&Aring;' scene=''>

<table><tr><td colspan='2'>[[3ph0]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/"aeromonas_liquefaciens"_kluyver_and_van_niel_1936 "aeromonas liquefaciens" kluyver and van niel 1936]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PH0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3PH0 FirstGlance]. <br>

</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=3ph0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ph0 OCA], [http://pdbe.org/3ph0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3ph0 RCSB], [http://www.ebi.ac.uk/pdbsum/3ph0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3ph0 ProSAT]</span></td></tr>

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== Publication Abstract from PubMed ==

BACKGROUND: The putative needle complex subunit AscF forms a ternary complex with the chaperones AscE and AscG in the type III secretion system of Aeromonas hydrophila so as to avoid premature assembly. Previously, we demonstrated that the C-terminal region of AscG (residues 62-116) in the hetero-molecular chaperone, AscE-AscG, is disordered and susceptible to limited protease digestion. METHODOLOGY/PRINCIPAL FINDINGS: Here, we report the crystal structure of the ordered AscG(1-61) region in complex with AscE at 2.4 A resolution. Helices alpha2 and alpha3 of AscE in the AscE-AscG(1-61) complex assumes a helix-turn-helix conformation in an anti-parallel fashion similar to that in apo AscE. However, in the presence of AscG, an additional N-terminal helix alpha1 in AscE (residues 4-12) is observed. PscG or YscG in the crystal structures of PscE-PscF-PscG or YscE-YscF-YscG, respectively, assumes a typical tetratricopeptide repeat (TPR) fold with three TPR repeats and one C-terminal capping helix. By comparison, AscG in AscE-AscG(1-61) comprises three anti-parallel helices that resembles the N-terminal TPR repeats in the corresponding region of PscG or YscG in PscE-PscF-PscG or YscE-YscF-YscG. Thermal denaturation of AscE-AscG and AscE-AscG(1-61) complexes demonstrates that the C-terminal disordered region does not contribute to the thermal stability of the overall complex. CONCLUSION/SIGNIFICANCE: The N-terminal region of the AscG in the AscE-AscG complex is ordered and assumes a structure similar to those in the corresponding regions of PscE-PscG-PscF or YscE-YscF-YscG complexes. While the C-terminal region of AscG in the AscE-AscG complex is disordered and will assume its structure only in the presence of the substrate AscF. We hypothesize that AscE act as a chaperone of the chaperone to keep AscG in a stable but partially disordered state for interaction with AscF.

 

Crystal structure of the heteromolecular chaperone, AscE-AscG, from the type III secretion system in Aeromonas hydrophila.,Chatterjee C, Kumar S, Chakraborty S, Tan YW, Leung KY, Sivaraman J, Mok YK PLoS One. 2011 Apr 29;6(4):e19208. PMID:21559439<ref>PMID:21559439</ref>

 

<references/>

[[Category: Aeromonas liquefaciens kluyver and van niel 1936]]

[[Category: Chakraborty, S]]

[[Category: Chatterjee, C]]

[[Category: Kumar, S]]

[[Category: Leung, K Y]]

[[Category: Mok, Y K]]

[[Category: Sivaraman, J]]

[[Category: Tan, Y W]]

[[Category: Type iii secretion system]]