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Journal of Biochemistry 2005 137(5):569-578; doi:10.1093/jb/mvi075
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© 2005 The Japanese Biochemical Society

Regular Paper

Stabilization Due to Dimer Formation of Phosphoribosyl Anthranilate Isomerase from Thermus thermophilus HB8: X-Ray Analysis and DSC Experiments

Junichiro Taka1, Kyoko Ogasahara2, Jeyaraman Jeyakanthan1, Naoki Kunishima1, Chizu Kuroishi1, Mitsuaki Sugahara1, Shigeyuki Yokoyama1,3,4 and Katsuhide Yutani1,*

1 RIKEN Harima Institute at SPring8, 1-1-1 Kohto, Mikazukicho, Sayo, Hyogo 679-5148; 2 Institute for Protein Research, Osaka University, 3-2 Yamadaoka, Suita, Osaka 565-0871; 3 RIKEN Genomic Sciences Center, 1-7-22 Suehiro, Tsurumi, Yokohama 230-0045; and 4 Graduate School of Science, the University of Tokyo, 7-3-1 Hongo, Bunkyoku, Tokyo 113-0033

The crystal structure of phosphoribosyl anthranilate isomerase (PRAI) from Thermus thermophilus HB8 (TtPRAI) was solved at 2.0 Å resolution. The overall structure of TtPRAI with a dimeric structure was quite similar to that of PRAI from Thermotoga maritima (TmPRAI). In order to elucidate the stabilization mechanism of TtPRAI, its physicochemical properties were examined using DSC, CD, and analytical centrifugation at various pHs in relation to the association-dissociation of the subunits. Based on the experimental results for TtPRAI and the structural information on TtPRAI and TmPRAI, we found that: (i) the denaturation of TtPRAI at acidic pH is correlated with the dissociation of its dimeric form; (ii) the hydrophobic interaction of TtPRAI in the monomer structure is slightly greater than that of TmPRAI, but dimer interface of the TmPRAI is remarkably greater; (iii) the contributions of hydrogen bonds and ion bonds to the stability are similar to each other; and (iv) destabilization due to the presence of cavities in TtPRAI is greater than that of TmPRAI in both the monomer and dimer structures.

* To whom correspondence should be addressed. Tel: +81-791-58-2937, Fax: +81-791-58-2917, E-mail: yutani@spring8.or.jp


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