1dxr
From Proteopedia
(New page: 200px<br /><applet load="1dxr" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dxr, resolution 2.00Å" /> '''PHOTOSYNTHETIC REACT...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1dxr.gif|left|200px]]<br /><applet load="1dxr" size=" | + | [[Image:1dxr.gif|left|200px]]<br /><applet load="1dxr" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1dxr, resolution 2.00Å" /> | caption="1dxr, resolution 2.00Å" /> | ||
'''PHOTOSYNTHETIC REACTION CENTER FROM RHODOPSEUDOMONAS VIRIDIS-HIS L168 PHE MUTANT (TERBUTRYN COMPLEX)'''<br /> | '''PHOTOSYNTHETIC REACTION CENTER FROM RHODOPSEUDOMONAS VIRIDIS-HIS L168 PHE MUTANT (TERBUTRYN COMPLEX)'''<br /> | ||
==Overview== | ==Overview== | ||
| - | It has previously been shown that replacement of the residue His L168 with | + | 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== | ==About this Structure== | ||
| - | 1DXR is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Blastochloris_viridis Blastochloris viridis] with FE2, SO4, HEC, BCB, BPB, MQ9, MST, NS5 and LDA as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1DXR is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Blastochloris_viridis Blastochloris viridis] with <scene name='pdbligand=FE2:'>FE2</scene>, <scene name='pdbligand=SO4:'>SO4</scene>, <scene name='pdbligand=HEC:'>HEC</scene>, <scene name='pdbligand=BCB:'>BCB</scene>, <scene name='pdbligand=BPB:'>BPB</scene>, <scene name='pdbligand=MQ9:'>MQ9</scene>, <scene name='pdbligand=MST:'>MST</scene>, <scene name='pdbligand=NS5:'>NS5</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=1DXR OCA]. |
==Reference== | ==Reference== | ||
| Line 14: | Line 14: | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Bibikova, M.]] | [[Category: Bibikova, M.]] | ||
| - | [[Category: Lancaster, C | + | [[Category: Lancaster, C R.D.]] |
[[Category: Michel, H.]] | [[Category: Michel, H.]] | ||
[[Category: Oesterhelt, D.]] | [[Category: Oesterhelt, D.]] | ||
| Line 31: | Line 31: | ||
[[Category: triazine inhibitor]] | [[Category: triazine inhibitor]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:21:37 2008'' |
Revision as of 10:21, 21 February 2008
|
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 with , , , , , , , and as ligands. 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 Feb 21 12:21:37 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
