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1dxr
From Proteopedia
| 1dxr, resolution 2.00Å () | |||||||||
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| Sites: | , , , , , , , , , , , , , , , , , , , , , , and | ||||||||
| Ligands: | , , , , , , , , | ||||||||
| Non-Standard Residues: | |||||||||
| Related: | 1prc, 2prc, 3prc, 4prc, 5prc, 6prc, 7prc | ||||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||
Contents |
PHOTOSYNTHETIC REACTION CENTER FROM RHODOPSEUDOMONAS VIRIDIS - HIS L168 PHE MUTANT (TERBUTRYN COMPLEX)
It has previously been shown that replacement of the residue His L168 with Phe (HL168F) in the Rhodopseudomonas viridis reaction center (RC) leads to an unprecedented drastic acceleration of the initial electron transfer rate. Here we describe the determination of the x-ray crystal structure at 2.00-A resolution of the HL168F RC. The electron density maps confirm that a hydrogen bond from the protein to the special pair is removed by this mutation. Compared with the wild-type RC, the acceptor of this hydrogen bond, the ring I acetyl group of the "special pair" bacteriochlorophyll, D(L), is rotated, and its acetyl oxygen is found 1.1 A closer to the bacteriochlorophyll-Mg(2+) of the other special pair bacteriochlorophyll, D(M). The rotation of this acetyl group and the increased interaction between the D(L) ring I acetyl oxygen and the D(M)-Mg(2+) provide the structural basis for the previously observed 80-mV decrease in the D(+)/D redox potential and the drastically increased rate of initial electron transfer to the accessory bacteriochlorophyll, B(A). The high quality of the electron density maps also allowed a reliable discussion of the mode of binding of the triazine herbicide terbutryn at the binding site of the secondary quinone, Q(B).
Structural basis of the drastically increased initial electron transfer rate in the reaction center from a Rhodopseudomonas viridis mutant described at 2.00-A resolution., Lancaster CR, Bibikova MV, Sabatino P, Oesterhelt D, Michel H, J Biol Chem. 2000 Dec 15;275(50):39364-8. PMID:11005826
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
About this Structure
1dxr is a 4 chain structure of Cytochrome c with sequence from Blastochloris viridis. Full crystallographic information is available from OCA.
See Also
Reference
- Lancaster CR, Bibikova MV, Sabatino P, Oesterhelt D, Michel H. Structural basis of the drastically increased initial electron transfer rate in the reaction center from a Rhodopseudomonas viridis mutant described at 2.00-A resolution. J Biol Chem. 2000 Dec 15;275(50):39364-8. PMID:11005826 doi:10.1074/jbc.M008225200
- Lancaster CR, Michel H. Refined crystal structures of reaction centres from Rhodopseudomonas viridis in complexes with the herbicide atrazine and two chiral atrazine derivatives also lead to a new model of the bound carotenoid. J Mol Biol. 1999 Feb 26;286(3):883-98. PMID:10024457 doi:10.1006/jmbi.1998.2532
- Lancaster CR, Michel H. The coupling of light-induced electron transfer and proton uptake as derived from crystal structures of reaction centres from Rhodopseudomonas viridis modified at the binding site of the secondary quinone, QB. Structure. 1997 Oct 15;5(10):1339-59. PMID:9351808
- Deisenhofer J, Epp O, Sinning I, Michel H. Crystallographic refinement at 2.3 A resolution and refined model of the photosynthetic reaction centre from Rhodopseudomonas viridis. J Mol Biol. 1995 Feb 24;246(3):429-57. PMID:7877166 doi:10.1006/jmbi.1994.0097
- Deisenhofer J, Michel H. The Photosynthetic Reaction Center from the Purple Bacterium Rhodopseudomonas viridis. Science. 1989 Sep 29;245(4925):1463-73. PMID:17776797 doi:10.1126/science.245.4925.1463
- Deisenhofer J, Epp O, Miki K, Huber R, Michel H. X-ray structure analysis of a membrane protein complex. Electron density map at 3 A resolution and a model of the chromophores of the photosynthetic reaction center from Rhodopseudomonas viridis. J Mol Biol. 1984 Dec 5;180(2):385-98. PMID:6392571
- Michel H. Three-dimensional crystals of a membrane protein complex. The photosynthetic reaction centre from Rhodopseudomonas viridis. J Mol Biol. 1982 Jul 5;158(3):567-72. PMID:7131557
- Spitz JA, Derrien V, Baciou L, Sebban P. Specific triazine resistance in bacterial reaction centers induced by a single mutation in the QA protein pocket. Biochemistry. 2005 Feb 1;44(4):1338-43. PMID:15667227 doi:10.1021/bi048701m
