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| <StructureSection load='3ph0' size='340' side='right'caption='[[3ph0]], [[Resolution|resolution]] 2.40Å' scene=''> | | <StructureSection load='3ph0' size='340' side='right'caption='[[3ph0]], [[Resolution|resolution]] 2.40Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
| <table><tr><td colspan='2'>[[3ph0]] is a 4 chain structure with sequence from [https://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 [https://proteopedia.org/fgij/fg.htm?mol=3PH0 FirstGlance]. <br> | | <table><tr><td colspan='2'>[[3ph0]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Aeromonas_hydrophila Aeromonas hydrophila]. 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 [https://proteopedia.org/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'>[https://proteopedia.org/fgij/fg.htm?mol=3ph0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ph0 OCA], [https://pdbe.org/3ph0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ph0 RCSB], [https://www.ebi.ac.uk/pdbsum/3ph0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ph0 ProSAT]</span></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]] 2.4Å</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=3ph0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ph0 OCA], [https://pdbe.org/3ph0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ph0 RCSB], [https://www.ebi.ac.uk/pdbsum/3ph0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ph0 ProSAT]</span></td></tr> |
| </table> | | </table> |
| <div style="background-color:#fffaf0;">
| | == Function == |
| == Publication Abstract from PubMed == | | [https://www.uniprot.org/uniprot/Q1EHA4_AERHY Q1EHA4_AERHY] |
| 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.
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| 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>
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| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| </div>
| |
| <div class="pdbe-citations 3ph0" style="background-color:#fffaf0;"></div>
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| == References ==
| |
| <references/>
| |
| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
| [[Category: Aeromonas liquefaciens kluyver and van niel 1936]] | | [[Category: Aeromonas hydrophila]] |
| [[Category: Large Structures]] | | [[Category: Large Structures]] |
| [[Category: Chakraborty, S]] | | [[Category: Chakraborty S]] |
| [[Category: Chatterjee, C]] | | [[Category: Chatterjee C]] |
| [[Category: Kumar, S]] | | [[Category: Kumar S]] |
| [[Category: Leung, K Y]] | | [[Category: Leung KY]] |
| [[Category: Mok, Y K]] | | [[Category: Mok YK]] |
| [[Category: Sivaraman, J]] | | [[Category: Sivaraman J]] |
| [[Category: Tan, Y W]] | | [[Category: Tan YW]] |
| [[Category: Chaperone]]
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| [[Category: Chaperones asce and ascg]]
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| [[Category: Type iii secretion system]]
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