1c2r
From Proteopedia
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| - | [[Image:1c2r.jpg|left|200px]] | + | [[Image:1c2r.jpg|left|200px]] |
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| - | '''MOLECULAR STRUCTURE OF CYTOCHROME C2 ISOLATED FROM RHODOBACTER CAPSULATUS DETERMINED AT 2.5 ANGSTROMS RESOLUTION''' | + | {{Structure |
| + | |PDB= 1c2r |SIZE=350|CAPTION= <scene name='initialview01'>1c2r</scene>, resolution 2.5Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=HEM:PROTOPORPHYRIN IX CONTAINING FE'>HEM</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''MOLECULAR STRUCTURE OF CYTOCHROME C2 ISOLATED FROM RHODOBACTER CAPSULATUS DETERMINED AT 2.5 ANGSTROMS RESOLUTION''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1C2R is a [ | + | 1C2R is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rhodobacter_capsulatus Rhodobacter capsulatus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1C2R OCA]. |
==Reference== | ==Reference== | ||
| - | Molecular structure of cytochrome c2 isolated from Rhodobacter capsulatus determined at 2.5 A resolution., Benning MM, Wesenberg G, Caffrey MS, Bartsch RG, Meyer TE, Cusanovich MA, Rayment I, Holden HM, J Mol Biol. 1991 Aug 5;220(3):673-85. PMID:[http:// | + | Molecular structure of cytochrome c2 isolated from Rhodobacter capsulatus determined at 2.5 A resolution., Benning MM, Wesenberg G, Caffrey MS, Bartsch RG, Meyer TE, Cusanovich MA, Rayment I, Holden HM, J Mol Biol. 1991 Aug 5;220(3):673-85. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/1651396 1651396] |
[[Category: Rhodobacter capsulatus]] | [[Category: Rhodobacter capsulatus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: electron transport protein (cytochrome)]] | [[Category: electron transport protein (cytochrome)]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:19:07 2008'' |
Revision as of 08:19, 20 March 2008
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| , resolution 2.5Å | |||||||
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
MOLECULAR STRUCTURE OF CYTOCHROME C2 ISOLATED FROM RHODOBACTER CAPSULATUS DETERMINED AT 2.5 ANGSTROMS RESOLUTION
Overview
The molecular structure of the cytochrome c2, isolated from the purple photosynthetic bacterium Rhodobacter capsulatus, has been solved to a nominal resolution of 2.5 A and refined to a crystallographic R-factor of 16.8% for all observed X-ray data. Crystals used for this investigation belong to the space group R32 with two molecules in the asymmetric unit and unit cell dimensions of a = b = 100.03 A, c = 162.10 A as expressed in the hexagonal setting. An interpretable electron density map calculated at 2.5 A resolution was obtained by the combination of multiple isomorphous replacement with four heavy atom derivatives, molecular averaging and solvent flattening. At this stage of the structural analysis the electron densities corresponding to the side-chains are well ordered except for several surface lysine, glutamate and aspartate residues. Like other c-type cytochromes, the secondary structure of the protein consists of five alpha-helices forming a basket around the heme prosthetic group with one heme edge exposed to the solvent. The overall alpha-carbon trace of the molecule is very similar to that observed for the bacterial cytochrome c2, isolated from Rhodospirillum rubrum, with the exception of a loop, delineated by amino acid residues 21 to 32, that forms a two stranded beta-sheet-like motif in the Rb. capsulatus protein. As observed in the eukaryotic cytochrome c proteins, but not in the cytochrome c2 from Rsp. rubrum, there are two evolutionarily conserved solvent molecules buried within the heme binding pocket.
About this Structure
1C2R is a Single protein structure of sequence from Rhodobacter capsulatus. Full crystallographic information is available from OCA.
Reference
Molecular structure of cytochrome c2 isolated from Rhodobacter capsulatus determined at 2.5 A resolution., Benning MM, Wesenberg G, Caffrey MS, Bartsch RG, Meyer TE, Cusanovich MA, Rayment I, Holden HM, J Mol Biol. 1991 Aug 5;220(3):673-85. PMID:1651396
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