1c2r
From Proteopedia
(New page: 200px<br /><applet load="1c2r" size="450" color="white" frame="true" align="right" spinBox="true" caption="1c2r, resolution 2.5Å" /> '''MOLECULAR STRUCTURE O...) |
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| - | [[Image:1c2r.jpg|left|200px]]<br /><applet load="1c2r" size=" | + | [[Image:1c2r.jpg|left|200px]]<br /><applet load="1c2r" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1c2r, resolution 2.5Å" /> | caption="1c2r, resolution 2.5Å" /> | ||
'''MOLECULAR STRUCTURE OF CYTOCHROME C2 ISOLATED FROM RHODOBACTER CAPSULATUS DETERMINED AT 2.5 ANGSTROMS RESOLUTION'''<br /> | '''MOLECULAR STRUCTURE OF CYTOCHROME C2 ISOLATED FROM RHODOBACTER CAPSULATUS DETERMINED AT 2.5 ANGSTROMS RESOLUTION'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The molecular structure of the cytochrome c2, isolated from the purple | + | 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== | ==About this Structure== | ||
| - | 1C2R is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rhodobacter_capsulatus Rhodobacter capsulatus] with HEM as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1C2R is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rhodobacter_capsulatus Rhodobacter capsulatus] with <scene name='pdbligand=HEM:'>HEM</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1C2R OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Rhodobacter capsulatus]] | [[Category: Rhodobacter capsulatus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Bartsch, R | + | [[Category: Bartsch, R G.]] |
| - | [[Category: Benning, M | + | [[Category: Benning, M M.]] |
| - | [[Category: Caffrey, M | + | [[Category: Caffrey, M S.]] |
| - | [[Category: Cusanovich, M | + | [[Category: Cusanovich, M A.]] |
| - | [[Category: Holden, H | + | [[Category: Holden, H M.]] |
| - | [[Category: Meyer, T | + | [[Category: Meyer, T E.]] |
[[Category: Rayment, I.]] | [[Category: Rayment, I.]] | ||
[[Category: Wesenberg, G.]] | [[Category: Wesenberg, G.]] | ||
| Line 24: | Line 24: | ||
[[Category: electron transport protein (cytochrome)]] | [[Category: electron transport protein (cytochrome)]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:01:51 2008'' |
Revision as of 10:01, 21 February 2008
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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 with as ligand. 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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