Issue 12, 2015

Oligomerization enhancement and two domain swapping mode detection for thermostable cytochrome c552via the elongation of the major hinge loop

Abstract

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.

Graphical abstract: Oligomerization enhancement and two domain swapping mode detection for thermostable cytochrome c552via the elongation of the major hinge loop

Supplementary files

Article information

Article type
Communication
Submitted
13 Aug. 2015
Accepted
29 Sept. 2015
First published
30 Sept. 2015

Mol. BioSyst., 2015,11, 3218-3221

Author version available

Oligomerization enhancement and two domain swapping mode detection for thermostable cytochrome c552via the elongation of the major hinge loop

C. Ren, S. Nagao, M. Yamanaka, H. Komori, Y. Shomura, Y. Higuchi and S. Hirota, Mol. BioSyst., 2015, 11, 3218 DOI: 10.1039/C5MB00545K

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