crystal structure of the heteromolecular chaperone, asce-ascg, from the type iii secretion system in aeromonas hydrophilaasce-ascg heteromolecular伴侣蛋白的晶体结构,从气单胞菌属的iii型分泌系统hydrophila.pdfVIP

Crystal Structure of the Heteromolecular Chaperone, AscE-AscG, from the Type III Secretion System in Aeromonas hydrophila Chiradip Chatterjee¤a, Sundramurthy Kumar¤b, Smarajit Chakraborty, Yih Wan Tan, Ka Yin Leung¤c, J. Sivaraman, Yu-Keung Mok* Department of Biological Sciences, National University of Singapore, Singapore Abstract 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 AscG1–61 region in complex with AscE ˚ at 2.4 A resolution. Helices a2 and a3 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 a1 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: T