2ccy

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spinqualitylabelsall models 2ccy, resolution 1.67Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

STRUCTURE OF FERRICYTOCHROME C(PRIME) FROM RHODOSPIRILLUM MOLISCHIANUM AT 1.67 ANGSTROMS RESOLUTION

Overview

The structure of ferricytochrome c' from Rhodospirillum molischianum has, been crystallographically refined to 1.67 A resolution using a combination, of reciprocal space and restrained least-squares refinement methods. The, final crystallographic R-factor for 30,533 reflections measured with I, greater than sigma (I) between infinity and 1.67 A is 0.188. The final, model incorporates 1944 unique protein atoms (of a total of 1972) together, with 194 bound solvent molecules. The structure has been analysed with, respect to its detailed conformational properties, secondary structural, features, temperature factor behavior, bound solvent sites, and heme, geometry. The asymmetric unit of the cytochrome c' crystal contains a, dimer composed of chemically identical 128-residue polypeptide chains., Although the refined structure shows the monomers to be very similar, examination of the differences that do occur allows an evaluation of how, different lattice contacts affect protein conformation and solvent, binding. In particular, comparison of solvent binding sites in the two, subunits allows identification of a common set that are not altered by, lattice interactions. The preservation of these solvent interactions in, different lattice environments suggests that they play a structural role, in protein stabilization in solution. The refined structure additionally, reveals some new features that relate to the ligand binding properties and, unusual mixed-spin state character of cytochrome c'. Finally, comparison, of the heme binding geometry in cytochrome c' and other structurally, unrelated c-type cytochromes shows that two alternative, but sterically, favorable, conformational variants occur among the seven examples, examined.

About this Structure

2CCY is a Single protein structure of sequence from Phaeospirillum molischianum with HEM as ligand. This structure superseeds the now removed PDB entry 1CCY. Full crystallographic information is available from OCA.

Reference

Structure of ferricytochrome c' from Rhodospirillum molischianum at 1.67 A resolution., Finzel BC, Weber PC, Hardman KD, Salemme FR, J Mol Biol. 1985 Dec 5;186(3):627-43. PMID:3005592

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