3PH0

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

Summary for 3PH0

Entry DOI	10.2210/pdb3ph0/pdb
Descriptor	AscE, AscG (3 entities in total)
Functional Keywords	type iii secretion system, chaperones asce and ascg, chaperone
Biological source	Aeromonas hydrophila More
Total number of polymer chains	4
Total formula weight	28666.70
Authors	Chatterjee, C.,Kumar, S.,Chakraborty, S.,Tan, Y.W.,Leung, K.Y.,Sivaraman, J.,Mok, Y.K. (deposition date: 2010-11-03, release date: 2011-07-20, Last modification date: 2024-03-20)
Primary citation	Chatterjee, C.,Kumar, S.,Chakraborty, S.,Tan, Y.W.,Leung, K.Y.,Sivaraman, J.,Mok, Y.K. Crystal structure of the heteromolecular chaperone, AscE-AscG, from the type III secretion system in Aeromonas hydrophila Plos One, 6:e19208-e19208, 2011 Cited by PubMed Abstract: 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. PubMed: 21559439 DOI: 10.1371/journal.pone.0019208 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2.4 Å)

Structure validation