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: 21559439DOI: 10.1371/journal.pone.0019208 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
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