4cjo | pdb_00004cjo

Spectroscopically-validated structure of ferrous cytochrome c prime from Alcaligenes xylosoxidans, reduced at 180K using X-rays

spinqualitylabelsall models 4cjo, resolution 1.55Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4cjo is a 1 chain structure with sequence from "achromobacter_xylosoxidans"_yabuuchi_and_ohyama_1971 "achromobacter xylosoxidans" yabuuchi and ohyama 1971. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: HEC NonStd Res: PCA Related: 4cjg Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [CYCP_ALCXX] Cytochrome c' is the most widely occurring bacterial c-type cytochrome. Cytochromes c' are high-spin proteins and the heme has no sixth ligand. Their exact function is not known. Publication Abstract from PubMed It is crucial to assign the correct redox and ligand states to crystal structures of proteins with an active redox centre to gain valid functional information and prevent the misinterpretation of structures. Single-crystal spectroscopies, particularly when applied in situ at macromolecular crystallography beamlines, allow spectroscopic investigations of redox and ligand states and the identification of reaction intermediates in protein crystals during the collection of structural data. Single-crystal resonance Raman spectroscopy was carried out in combination with macromolecular crystallography on Swiss Light Source beamline X10SA using cytochrome c' from Alcaligenes xylosoxidans. This allowed the fingerprinting and validation of different redox and ligand states, identification of vibrational modes and identification of intermediates together with monitoring of radiation-induced changes. This combined approach provides a powerful tool to obtain complementary data and correctly assign the true oxidation and ligand state(s) in redox-protein crystals. Fingerprinting redox and ligand states in haemprotein crystal structures using resonance Raman spectroscopy.,Kekilli D, Dworkowski FS, Pompidor G, Fuchs MR, Andrew CR, Antonyuk S, Strange RW, Eady RR, Hasnain SS, Hough MA Acta Crystallogr D Biol Crystallogr. 2014 May;70(Pt 5):1289-96. doi:, 10.1107/S1399004714004039. Epub 2014 Apr 29. PMID:24816098 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Cytochrome c

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