3u99

The experimental X-ray structure of the new diheme cytochrome type c from Shewanella baltica OS155 sb-DHCThe experimental X-ray structure of the new diheme cytochrome type c from Shewanella baltica OS155 sb-DHC

Structural highlights 3u99 is a 1 chain structure with sequence from Shewanella baltica OS155. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.146Å Ligands: Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A3CZ62_SHEB5 Publication Abstract from PubMed Multiheme cytochromes c (cyts c) are c-type cyts characterized by non-standard structural and spectroscopic properties. The relative disposition of the heme cofactors in the core of these proteins is conserved and they can be classified from their geometry in two main groups. In one group the porphyrin planes are arranged in a perpendicular fashion, while in the other they are parallel. Orientation of the heme groups is a key factor that regulates the intramolecular electron transfer pathway. A 16.5 kDa diheme cyt c, isolated from the bacterium Shewanella baltica OS155 (Sb-DHC), was cloned and expressed in E. coli and its structure was investigated by X-ray crystallography. Using high-resolution data (1.14 A) collected at ELETTRA (Trieste), the crystal structure, with an orthorhombic cell (a = 40.81, b = 42.97, c = 82.07 A), was solved using the homologous diheme from Rhodobacter sphaeroides (Rs-DHC) as the initial model. The electron density map of the refined structure (Rfact of 13.8% and Rfree of 15.4%) shows a two domain structure connected by a central unstructured region (N72-G87). The Sb-DHC, like its homologue (Rs-DHC), folds into a new cyt c class: the N-terminal globular domain, with its three alpha-helices, belongs to class I of c-type cyts, while the C-terminal domain includes a rare pi-helix. The metal centre of the c-type heme groups is axially coordinated by two His residues and it is covalently bound to the protein through two Cys bonds. High-resolution crystal structure of the recombinant diheme cytochrome c from Shewanella baltica (OS155).,De March M, Di Rocco G, Hickey N, Geremia S J Biomol Struct Dyn. 2014 Feb 21. PMID:24559494 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Cytochrome C 3D structures

spinqualitylabelsall models 3u99, resolution 1.15Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image