4zid

Dimeric Hydrogenobacter thermophilus cytochrome c552 obtained from Escherichia coli

spinqualitylabelsall models 4zid, resolution 1.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4zid is a 1 chain structure with sequence from Hydrogenobacter thermophilus TK-6. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.8Å Ligands: HEC Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function CY552_HYDTT Reacts with hydrogenase. Publication Abstract from PubMed Knowledge on domain swapping in vitro is increasing, but domain swapping may not occur regularly in vivo, and its information in cells is limited. Herein, we show that domain-swapped oligomers of a thermostable c-type cytochrome, Hydrogenobacter thermophilus cyt c552, are formed in E. coli which expresses cyt c552. The region containing the N-terminal alpha-helix and heme was domain-swapped between protomers in the dimer formed in E. coli. The amount of cyt c552 oligomers increased in E. coli as the cyt c552 concentration was increased, whereas that of high-order oligomers decreased in the order of decrease in protein stability, indicating that domain swapping decreases in cells when the protein stability decreases. Apo cyt c552 was detected in the cyt c552 oligomer formed in E. coli, but not in that of the A5F/M11V/Y32F/Y41E/I76V mutant. The cyt c552 oligomer containing its apo protein may form at the periplasm, since the apo protein detected by mass measurements did not contain the signal peptide. These results show that domain-swapped cyt c552 oligomers were formed in E. coli, owing to the stability of the transient oligomer containing the apo protein before heme attachment. This is an indication that exceedingly stable proteins may have disadvantages forming domain-swapped oligomers in cells. Domain swapping oligomerization of thermostable c-type cytochrome in E. coli cells.,Hayashi Y, Yamanaka M, Nagao S, Komori H, Higuchi Y, Hirota S Sci Rep. 2016 Feb 3;6:19334. doi: 10.1038/srep19334. PMID:26838805 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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