1m3x
From Proteopedia
(New page: 200px<br /><applet load="1m3x" size="450" color="white" frame="true" align="right" spinBox="true" caption="1m3x, resolution 2.55Å" /> '''Photosynthetic React...) |
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| - | [[Image:1m3x.gif|left|200px]]<br /><applet load="1m3x" size=" | + | [[Image:1m3x.gif|left|200px]]<br /><applet load="1m3x" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1m3x, resolution 2.55Å" /> | caption="1m3x, resolution 2.55Å" /> | ||
'''Photosynthetic Reaction Center From Rhodobacter Sphaeroides'''<br /> | '''Photosynthetic Reaction Center From Rhodobacter Sphaeroides'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The structure of the reaction center from Rhodobacter sphaeroides has been | + | The structure of the reaction center from Rhodobacter sphaeroides has been solved by using x-ray diffraction at a 2.55-A resolution limit. Three lipid molecules that lie on the surface of the protein are resolved in the electron density maps. In addition to a cardiolipin that has previously been reported [McAuley, K. E., Fyfe, P. K., Ridge, J. P., Isaacs, N. W., Cogdell, R. J. & Jones, M. R. (1999) Proc. Natl. Acad. Sci. USA 96, 14706-14711], two other major lipids of the cell membrane are found, a phosphatidylcholine and a glucosylgalactosyl diacylglycerol. The presence of these three lipids has been confirmed by laser mass spectroscopy. The lipids are located in the hydrophobic region of the protein surface and interact predominately with hydrophobic amino acids, in particular aromatic residues. Although the cardiolipin is over 15 A from the cofactors, the other two lipids are in close contact with the cofactors and may contribute to the difference in energetics for the two branches of cofactors that is primarily responsible for the asymmetry of electron transfer. The glycolipid is 3.5 A from the active bacteriochlorophyll monomer and shields this cofactor from the solvent in contrast to a much greater exposed surface evident for the inactive bacteriochlorophyll monomer. The phosphate atom of phosphatidylcholine is 6.5 A from the inactive bacteriopheophytin, and the associated electrostatic interactions may contribute to electron transfer rates involving this cofactor. Overall, the lipids span a distance of approximately 30 A, which is consistent with a bilayer-like arrangement suggesting the presence of an "inner shell" of lipids around membrane proteins that is critical for membrane function. |
==About this Structure== | ==About this Structure== | ||
| - | 1M3X is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Rhodobacter_sphaeroides Rhodobacter sphaeroides] with FE, CL, BCL, BPH, U10, SPO, CDL, PC1 and GGD as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1M3X is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Rhodobacter_sphaeroides Rhodobacter sphaeroides] with <scene name='pdbligand=FE:'>FE</scene>, <scene name='pdbligand=CL:'>CL</scene>, <scene name='pdbligand=BCL:'>BCL</scene>, <scene name='pdbligand=BPH:'>BPH</scene>, <scene name='pdbligand=U10:'>U10</scene>, <scene name='pdbligand=SPO:'>SPO</scene>, <scene name='pdbligand=CDL:'>CDL</scene>, <scene name='pdbligand=PC1:'>PC1</scene> and <scene name='pdbligand=GGD:'>GGD</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M3X OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Rhodobacter sphaeroides]] | [[Category: Rhodobacter sphaeroides]] | ||
| - | [[Category: Allen, J | + | [[Category: Allen, J P.]] |
[[Category: Brune, D.]] | [[Category: Brune, D.]] | ||
[[Category: Camara-Artigas, A.]] | [[Category: Camara-Artigas, A.]] | ||
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[[Category: membrane protein]] | [[Category: membrane protein]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:51:10 2008'' |
Revision as of 11:51, 21 February 2008
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Photosynthetic Reaction Center From Rhodobacter Sphaeroides
Overview
The structure of the reaction center from Rhodobacter sphaeroides has been solved by using x-ray diffraction at a 2.55-A resolution limit. Three lipid molecules that lie on the surface of the protein are resolved in the electron density maps. In addition to a cardiolipin that has previously been reported [McAuley, K. E., Fyfe, P. K., Ridge, J. P., Isaacs, N. W., Cogdell, R. J. & Jones, M. R. (1999) Proc. Natl. Acad. Sci. USA 96, 14706-14711], two other major lipids of the cell membrane are found, a phosphatidylcholine and a glucosylgalactosyl diacylglycerol. The presence of these three lipids has been confirmed by laser mass spectroscopy. The lipids are located in the hydrophobic region of the protein surface and interact predominately with hydrophobic amino acids, in particular aromatic residues. Although the cardiolipin is over 15 A from the cofactors, the other two lipids are in close contact with the cofactors and may contribute to the difference in energetics for the two branches of cofactors that is primarily responsible for the asymmetry of electron transfer. The glycolipid is 3.5 A from the active bacteriochlorophyll monomer and shields this cofactor from the solvent in contrast to a much greater exposed surface evident for the inactive bacteriochlorophyll monomer. The phosphate atom of phosphatidylcholine is 6.5 A from the inactive bacteriopheophytin, and the associated electrostatic interactions may contribute to electron transfer rates involving this cofactor. Overall, the lipids span a distance of approximately 30 A, which is consistent with a bilayer-like arrangement suggesting the presence of an "inner shell" of lipids around membrane proteins that is critical for membrane function.
About this Structure
1M3X is a Protein complex structure of sequences from Rhodobacter sphaeroides with , , , , , , , and as ligands. Full crystallographic information is available from OCA.
Reference
Interactions between lipids and bacterial reaction centers determined by protein crystallography., Camara-Artigas A, Brune D, Allen JP, Proc Natl Acad Sci U S A. 2002 Aug 20;99(17):11055-60. Epub 2002 Aug 7. PMID:12167672
Page seeded by OCA on Thu Feb 21 13:51:10 2008
Categories: Protein complex | Rhodobacter sphaeroides | Allen, J P. | Brune, D. | Camara-Artigas, A. | BCL | BPH | CDL | CL | FE | GGD | PC1 | SPO | U10 | Alpha helix | Membrane protein
