Crystal structure of the heteromolecular chaperone, AscE-AscG, from the type III secretion system in Aeromonas hydrophila.

<h4>Background</h4>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 62-11...

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Autores principales:	Chiradip Chatterjee, Sundramurthy Kumar, Smarajit Chakraborty, Yih Wan Tan, Ka Yin Leung, J Sivaraman, Yu-Keung Mok
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Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2011
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/680e146151a5443a853a01a62a8de0aa
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spelling	oai:doaj.org-article:680e146151a5443a853a01a62a8de0aa2021-11-18T06:54:46ZCrystal structure of the heteromolecular chaperone, AscE-AscG, from the type III secretion system in Aeromonas hydrophila.1932-620310.1371/journal.pone.0019208https://doaj.org/article/680e146151a5443a853a01a62a8de0aa2011-04-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/21559439/pdf/?tool=EBIhttps://doaj.org/toc/1932-6203<h4>Background</h4>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.<h4>Methodology/principal findings</h4>Here, we report the crystal structure of the ordered AscG(1-61) region in complex with AscE at 2.4 Å resolution. Helices α2 and α3 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 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-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.<h4>Conclusion/significance</h4>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.Chiradip ChatterjeeSundramurthy KumarSmarajit ChakrabortyYih Wan TanKa Yin LeungJ SivaramanYu-Keung MokPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 6, Iss 4, p e19208 (2011)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Chiradip Chatterjee Sundramurthy Kumar Smarajit Chakraborty Yih Wan Tan Ka Yin Leung J Sivaraman Yu-Keung Mok Crystal structure of the heteromolecular chaperone, AscE-AscG, from the type III secretion system in Aeromonas hydrophila.
description	<h4>Background</h4>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.<h4>Methodology/principal findings</h4>Here, we report the crystal structure of the ordered AscG(1-61) region in complex with AscE at 2.4 Å resolution. Helices α2 and α3 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 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-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.<h4>Conclusion/significance</h4>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.
format	article
author	Chiradip Chatterjee Sundramurthy Kumar Smarajit Chakraborty Yih Wan Tan Ka Yin Leung J Sivaraman Yu-Keung Mok
author_facet	Chiradip Chatterjee Sundramurthy Kumar Smarajit Chakraborty Yih Wan Tan Ka Yin Leung J Sivaraman Yu-Keung Mok
author_sort	Chiradip Chatterjee
title	Crystal structure of the heteromolecular chaperone, AscE-AscG, from the type III secretion system in Aeromonas hydrophila.
title_short	Crystal structure of the heteromolecular chaperone, AscE-AscG, from the type III secretion system in Aeromonas hydrophila.
title_full	Crystal structure of the heteromolecular chaperone, AscE-AscG, from the type III secretion system in Aeromonas hydrophila.
title_fullStr	Crystal structure of the heteromolecular chaperone, AscE-AscG, from the type III secretion system in Aeromonas hydrophila.
title_full_unstemmed	Crystal structure of the heteromolecular chaperone, AscE-AscG, from the type III secretion system in Aeromonas hydrophila.
title_sort	crystal structure of the heteromolecular chaperone, asce-ascg, from the type iii secretion system in aeromonas hydrophila.
publisher	Public Library of Science (PLoS)
publishDate	2011
url	https://doaj.org/article/680e146151a5443a853a01a62a8de0aa
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Crystal structure of the heteromolecular chaperone, AscE-AscG, from the type III secretion system in Aeromonas hydrophila.

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