5AUR

Hydrogenobacter thermophilus cytochrome c552 dimer formed by domain swapping at N-terminal region

Summary for 5AUR

• Entry DOI: 10.2210/pdb5aur/pdb
• Related: 3VYM 5AUS
• Descriptor: Cytochrome c-552, HEME C, IODIDE ION, ... (4 entities in total)
• Functional Keywords: electron transfer, electron transport
• Biological source: Hydrogenobacter thermophilus (strain DSM 6534 / IAM 12695 / TK-6)
• Total number of polymer chains: 4
• Total formula weight: 38898.63

Authors

Ren, C.,Nagao, S.,Yamanaka, M.,Kamikubo, H.,Komori, H.,Shomura, Y.,Higuchi, Y.,Hirota, S. (deposition date: 2015-06-08, release date: 2015-10-21, Last modification date: 2024-11-13)

Primary citation

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 c552via the elongation of the major hinge loop.
Mol Biosyst, 11:3218-3221, 2015

PubMed 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.

PubMed: 26451671
DOI: 10.1039/c5mb00545k

Experimental method

X-RAY DIFFRACTION (1.26 Å)