Oligomerization enhancement and two domain swapping mode detection for thermostable cytochrome c552 via the elongation of the major hinge loop.
作者信息
Ren Chunguang, Nagao Satoshi, Yamanaka Masaru, Komori Hirofumi, Shomura Yasuhito, Higuchi Yoshiki, Hirota Shun
机构信息
Graduate School of Materials Science, Nara Institute of Science and Technology, 8916-5 Takayama, Ikoma, Nara 630-0192, Japan.
Faculty of Education, Kagawa University, 1-1 Saiwai, Takamatsu, Kagawa 760-8522, Japan.
出版信息
Mol Biosyst. 2015 Dec;11(12):3218-21. doi: 10.1039/c5mb00545k.
High-order oligomers of Hydrogenobacter thermophilus cytochrome c552 increased with the insertion of more Gly residues between Ala18 and Lys19 at the major hinge loop of the wild-type protein. N-Terminal domain swapping and C-terminal domain swapping were elucidated by using X-ray crystallography for the mutant with the insertion of three Gly residues at the hinge loop.
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