Please use this identifier to cite or link to this item: https://doi.org/10.1371/journal.pone.0019208
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dc.titleCrystal structure of the heteromolecular chaperone, AscE-AscG, from the type III secretion system in Aeromonas hydrophila
dc.contributor.authorChatterjee, C.
dc.contributor.authorKumar, S.
dc.contributor.authorChakraborty, S.
dc.contributor.authorTan, Y.W.
dc.contributor.authorLeung, K.Y.
dc.contributor.authorSivaraman, J.
dc.contributor.authorMok, Y.-K.
dc.date.accessioned2014-12-12T07:10:26Z
dc.date.available2014-12-12T07:10:26Z
dc.date.issued2011
dc.identifier.citationChatterjee, C., Kumar, S., Chakraborty, S., Tan, Y.W., Leung, K.Y., Sivaraman, J., Mok, Y.-K. (2011). Crystal structure of the heteromolecular chaperone, AscE-AscG, from the type III secretion system in Aeromonas hydrophila. PLoS ONE 6 (4) : -. ScholarBank@NUS Repository. https://doi.org/10.1371/journal.pone.0019208
dc.identifier.issn19326203
dc.identifier.urihttp://scholarbank.nus.edu.sg/handle/10635/115049
dc.description.abstractBackground: 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 AscG1-61 region in complex with AscE at 2.4 Å resolution. Helices α2 and α3 of AscE in the AscE-AscG1-61 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 α1 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-AscG1-61 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-AscG1-61 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. © 2011 Chatterjee et al.
dc.description.urihttp://libproxy1.nus.edu.sg/login?url=http://dx.doi.org/10.1371/journal.pone.0019208
dc.sourceScopus
dc.typeArticle
dc.contributor.departmentBIOLOGICAL SCIENCES
dc.contributor.departmentLIFE SCIENCES INSTITUTE
dc.description.doi10.1371/journal.pone.0019208
dc.description.sourcetitlePLoS ONE
dc.description.volume6
dc.description.issue4
dc.description.page-
dc.identifier.isiut000290024700103
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