2ccy
From Proteopedia
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[[Image:2ccy.jpg|left|200px]] | [[Image:2ccy.jpg|left|200px]] | ||
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| - | + | {{STRUCTURE_2ccy| PDB=2ccy | SCENE= }} | |
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'''STRUCTURE OF FERRICYTOCHROME C(PRIME) FROM RHODOSPIRILLUM MOLISCHIANUM AT 1.67 ANGSTROMS RESOLUTION''' | '''STRUCTURE OF FERRICYTOCHROME C(PRIME) FROM RHODOSPIRILLUM MOLISCHIANUM AT 1.67 ANGSTROMS RESOLUTION''' | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2CCY is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Phaeospirillum_molischianum Phaeospirillum molischianum]. This structure supersedes the now removed PDB entry | + | 2CCY is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Phaeospirillum_molischianum Phaeospirillum molischianum]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1ccy 1ccy]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CCY OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Salemme, F R.]] | [[Category: Salemme, F R.]] | ||
[[Category: Weber, P C.]] | [[Category: Weber, P C.]] | ||
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Revision as of 18:50, 3 May 2008
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. This structure supersedes 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 Page seeded by OCA on Sat May 3 21:50:41 2008
