1dxr
From Proteopedia
| Line 1: | Line 1: | ||
| - | [[Image:1dxr.gif|left|200px]] | + | [[Image:1dxr.gif|left|200px]] |
| - | + | ||
| - | '''PHOTOSYNTHETIC REACTION CENTER FROM RHODOPSEUDOMONAS VIRIDIS-HIS L168 PHE MUTANT (TERBUTRYN COMPLEX)''' | + | {{Structure |
| + | |PDB= 1dxr |SIZE=350|CAPTION= <scene name='initialview01'>1dxr</scene>, resolution 2.00Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=HEC:HEME+C'>HEC</scene>, <scene name='pdbligand=BCB:BACTERIOCHLOROPHYLL+B'>BCB</scene>, <scene name='pdbligand=BPB:BACTERIOPHEOPHYTIN+B'>BPB</scene>, <scene name='pdbligand=MQ9:MENAQUINONE-9'>MQ9</scene>, <scene name='pdbligand=MST:2-T-BUTYLAMINO-4-ETHYLAMINO-6-METHYLTHIO-S-TRIAZINE'>MST</scene>, <scene name='pdbligand=NS5:DIHYDRO-NEUROSPORENE'>NS5</scene> and <scene name='pdbligand=LDA:LAURYL DIMETHYLAMINE-N-OXIDE'>LDA</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''PHOTOSYNTHETIC REACTION CENTER FROM RHODOPSEUDOMONAS VIRIDIS-HIS L168 PHE MUTANT (TERBUTRYN COMPLEX)''' | ||
| + | |||
==Overview== | ==Overview== | ||
| Line 7: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
| - | 1DXR is a [ | + | 1DXR is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Blastochloris_viridis Blastochloris viridis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DXR OCA]. |
==Reference== | ==Reference== | ||
| - | 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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/11005826 11005826] |
[[Category: Blastochloris viridis]] | [[Category: Blastochloris viridis]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
| Line 31: | Line 40: | ||
[[Category: triazine inhibitor]] | [[Category: triazine inhibitor]] | ||
| - | ''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 10:46:13 2008'' |
Revision as of 08:46, 20 March 2008
| |||||||
| , resolution 2.00Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , , , , , , and | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
PHOTOSYNTHETIC REACTION CENTER FROM RHODOPSEUDOMONAS VIRIDIS-HIS L168 PHE MUTANT (TERBUTRYN COMPLEX)
Overview
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).
About this Structure
1DXR is a Protein complex structure of sequences from Blastochloris viridis. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Thu Mar 20 10:46:13 2008
Categories: Blastochloris viridis | Protein complex | Bibikova, M. | Lancaster, C R.D. | Michel, H. | Oesterhelt, D. | Sabatino, P. | BCB | BPB | FE2 | HEC | LDA | MQ9 | MST | NS5 | SO4 | Photosynthetic reaction center | Secondary quinone (qb) | Triazine inhibitor
