1pcr
From Proteopedia
(New page: 200px<br /><applet load="1pcr" size="450" color="white" frame="true" align="right" spinBox="true" caption="1pcr, resolution 2.65Å" /> '''STRUCTURE OF THE PHO...) |
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| - | [[Image:1pcr.gif|left|200px]]<br /><applet load="1pcr" size=" | + | [[Image:1pcr.gif|left|200px]]<br /><applet load="1pcr" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1pcr, resolution 2.65Å" /> | caption="1pcr, resolution 2.65Å" /> | ||
'''STRUCTURE OF THE PHOTOSYNTHETIC REACTION CENTRE FROM RHODOBACTER SPHAEROIDES AT 2.65 ANGSTROMS RESOLUTION: COFACTORS AND PROTEIN-COFACTOR INTERACTIONS'''<br /> | '''STRUCTURE OF THE PHOTOSYNTHETIC REACTION CENTRE FROM RHODOBACTER SPHAEROIDES AT 2.65 ANGSTROMS RESOLUTION: COFACTORS AND PROTEIN-COFACTOR INTERACTIONS'''<br /> | ||
==Overview== | ==Overview== | ||
| - | BACKGROUND: Photosynthetic reaction centres (RCs) catalyze light-driven | + | BACKGROUND: Photosynthetic reaction centres (RCs) catalyze light-driven electron, transport across photosynthetic membranes. The photosynthetic bacterium Rhodobacter, sphaeroides is often used for studies of RCs, and three groups have determined the structure of its reaction centre. There are discrepancies between these structures, however, and to resolve these we have determined the structure to higher resolution than before, using a new crystal form. RESULTS: The new structure provides a more detailed description of the Rb. sphaeroides RC, and allows us to compare it with the structure of the RC from Rhodopseudomonas viridis. We find no evidence to support most of the published differences in cofactor binding between the RCs from Rps. viridis and Rb. sphaeroides. Generally, the mode of cofactor binding is conserved, particularly along the electron transfer pathway. Substantial differences are only found at ring V of one bacteriochlorophyll of the 'special pair' and for the secondary quinone, QB. A water chain with a length of about 23 A including 14 water molecules extends from the QB to the cytoplasmic side of the RC. CONCLUSIONS: The cofactor arrangement and the mode of binding to the protein seem to be very similar among the non-sulphur bacterial photosynthetic RCs. The functional role of the displaced QB molecule, which might be present as quinol, rather than quinone, is not yet clear. The newly discovered water chain to the QB binding site suggests a pathway for the protonation of the secondary quinone QB. |
==About this Structure== | ==About this Structure== | ||
| - | 1PCR 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, PO4, BCL, BPH, U10, SPO and LDA as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1PCR 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=PO4:'>PO4</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> and <scene name='pdbligand=LDA:'>LDA</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PCR OCA]. |
==Reference== | ==Reference== | ||
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[[Category: photosynthetic reaction center]] | [[Category: photosynthetic reaction center]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:27:30 2008'' |
Revision as of 12:27, 21 February 2008
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STRUCTURE OF THE PHOTOSYNTHETIC REACTION CENTRE FROM RHODOBACTER SPHAEROIDES AT 2.65 ANGSTROMS RESOLUTION: COFACTORS AND PROTEIN-COFACTOR INTERACTIONS
Overview
BACKGROUND: Photosynthetic reaction centres (RCs) catalyze light-driven electron, transport across photosynthetic membranes. The photosynthetic bacterium Rhodobacter, sphaeroides is often used for studies of RCs, and three groups have determined the structure of its reaction centre. There are discrepancies between these structures, however, and to resolve these we have determined the structure to higher resolution than before, using a new crystal form. RESULTS: The new structure provides a more detailed description of the Rb. sphaeroides RC, and allows us to compare it with the structure of the RC from Rhodopseudomonas viridis. We find no evidence to support most of the published differences in cofactor binding between the RCs from Rps. viridis and Rb. sphaeroides. Generally, the mode of cofactor binding is conserved, particularly along the electron transfer pathway. Substantial differences are only found at ring V of one bacteriochlorophyll of the 'special pair' and for the secondary quinone, QB. A water chain with a length of about 23 A including 14 water molecules extends from the QB to the cytoplasmic side of the RC. CONCLUSIONS: The cofactor arrangement and the mode of binding to the protein seem to be very similar among the non-sulphur bacterial photosynthetic RCs. The functional role of the displaced QB molecule, which might be present as quinol, rather than quinone, is not yet clear. The newly discovered water chain to the QB binding site suggests a pathway for the protonation of the secondary quinone QB.
About this Structure
1PCR is a Protein complex structure of sequences from Rhodobacter sphaeroides with , , , , , and as ligands. Full crystallographic information is available from OCA.
Reference
Structure of the photosynthetic reaction centre from Rhodobacter sphaeroides at 2.65 A resolution: cofactors and protein-cofactor interactions., Ermler U, Fritzsch G, Buchanan SK, Michel H, Structure. 1994 Oct 15;2(10):925-36. PMID:7866744
Page seeded by OCA on Thu Feb 21 14:27:30 2008
Categories: Protein complex | Rhodobacter sphaeroides | Ermler, U. | Fritzsch, G. | Michel, H. | BCL | BPH | FE | LDA | PO4 | SPO | U10 | Photosynthetic reaction center
