ニュース

2015年10月16日 掲載 (Published 10/16/2015)


「Biophysics and Physicobiology」に Eiji Kanamori et al." Structural comparison between the open and closed forms of citrate synthase from Thermus thermophilus HB8"を掲載

日本生物物理学会欧文誌[Biophysics and Physicobiology]に以下の論文が新規掲載されました。

Eiji Kanamori, Shin-ichi Kawaguchi, Seiki Kuramitsu, Tsutomu Kouyama and Midori Murakami
” Structural comparison between the open and closed forms of citrate synthase from Thermus thermophilus HB8”

【Significance】
Conformational change of citrate synthase

In this study, we determined and compared crystal structures of citrate synthase (CS) from T. thermophilus in open and closed states. Structural comparisons between them revealed that a large domain movement is evoked upon citrate binding to the active site. In addition, a twisting motion in the hinge region connecting the large and small domains is crucial for closing the active site. We propose that these distinct motions are essential for catalytic function and that the conservation of the three-residue His-Gly-Gly array around the hinge region would help elucidate the sequential ordered bi-bi catalytic mechanism of CS from microorganisms.


Biophysics and Physicobiology, Vol.12, pp. 47-56

URL:http://doi.org/10.2142/biophysico.12.0_47