Structural highlights
Function
CY552_HYDTT Reacts with hydrogenase.
Publication Abstract from PubMed
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.
Oligomerization enhancement and two domain swapping mode detection for thermostable cytochrome cvia the elongation of the major hinge loop.,Ren C, Nagao S, Yamanaka M, Komori H, Shomura Y, Higuchi Y, Hirota S Mol Biosyst. 2015 Oct 9. PMID:26451671[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Ren C, Nagao S, Yamanaka M, Komori H, Shomura Y, Higuchi Y, Hirota S. Oligomerization enhancement and two domain swapping mode detection for thermostable cytochrome cvia the elongation of the major hinge loop. Mol Biosyst. 2015 Oct 9. PMID:26451671 doi:http://dx.doi.org/10.1039/c5mb00545k
