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| | {{STRUCTURE_2ccy| PDB=2ccy | SCENE= }} | | {{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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| - | ==Overview==
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| - | 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.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_3005592}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 3005592 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_3005592}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Salemme, F R.]] | | [[Category: Salemme, F R.]] |
| | [[Category: Weber, P C.]] | | [[Category: Weber, P C.]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 21:50:41 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 01:15:02 2008'' |
Revision as of 22:15, 28 July 2008
Template:STRUCTURE 2ccy
STRUCTURE OF FERRICYTOCHROME C(PRIME) FROM RHODOSPIRILLUM MOLISCHIANUM AT 1.67 ANGSTROMS RESOLUTION
Template:ABSTRACT PUBMED 3005592
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 Tue Jul 29 01:15:02 2008
