6k7c

Dimeric Shewanella violacea cytochrome c5Dimeric Shewanella violacea cytochrome c5

Structural highlights 6k7c is a 2 chain structure with sequence from Shewanella violacea. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.15Å Ligands: , Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function D4ZE39_SHEVD Publication Abstract from PubMed Many c-type cytochromes (cyts) can form domain-swapped oligomers. The positively charged Hydrogenobacter thermophilus (HT) cytochrome (cyt) c(552) forms domain-swapped oligomers during expression in the Escherichia coli (E. coli) expression system, but the factors influencing the oligomerization remain unrevealed. Here, we found that the dimer of the negatively charged Shewanella violacea (SV) cyt c(5) exhibits a domain-swapped structure, in which the N-terminal helix is exchanged between protomers, similar to the structures of the HT cyt c(552) and Pseudomonas aeruginosa (PA) cyt c(551) domain-swapped dimers. Positively charged horse cyt c and HT cyt c(552) domain swapped during expression in E. coli, whereas negatively charged PA cyt c(551) and SV cyt c(5) did not. Oligomers were formed during expression in E. coli for HT cyt c(552) attached to either a co- or post-translational signal peptide for transportation through the cytoplasm membrane, but not for PA cyt c(551) attached to either signal peptide. HT cyt c(552) formed oligomers in E. coli in the presence and absence of rare codons. More oligomers were obtained from the in vitro folding of horse cyt c and HT cyt c(552) by the addition of negatively charged liposomes during folding, whereas the amount of oligomers for the in vitro folding of PA cyt c(551) and SV cyt c(5) did not change significantly by the addition. These results indicate that the protein surface charge affects the oligomerization of c-type cyts in cells; positively charged c-type cyts assemble on a negatively charged membrane, inducing formation of domain-swapped oligomers during folding. Protein surface charge effect on 3D domain swapping in cells for c-type cytochromes.,Yang H, Yamanaka M, Nagao S, Yasuhara K, Shibata N, Higuchi Y, Hirota S Biochim Biophys Acta Proteins Proteom. 2019 Nov;1867(11):140265. doi: , 10.1016/j.bbapap.2019.140265. Epub 2019 Aug 19. PMID:31437585 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Cytochrome C 3D structures

spinqualitylabelsall models 6k7c, resolution 1.15Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image