5aur

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

spinqualitylabelsall models 5aur, resolution 1.26Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5aur is a 4 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: HEC, IOD Related: 3vym, 5aus Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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