1dv6: Difference between revisions
New page: left|200px<br /><applet load="1dv6" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dv6, resolution 2.50Å" /> '''PHOTOSYNTHETIC REACT... |
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[[Image:1dv6.gif|left|200px]]<br /><applet load="1dv6" size=" | [[Image:1dv6.gif|left|200px]]<br /><applet load="1dv6" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1dv6, resolution 2.50Å" /> | caption="1dv6, resolution 2.50Å" /> | ||
'''PHOTOSYNTHETIC REACTION CENTER FROM RHODOBACTER SPHAEROIDES IN THE CHARGE-NEUTRAL DQAQB STATE WITH THE PROTON TRANSFER INHIBITOR ZN2+'''<br /> | '''PHOTOSYNTHETIC REACTION CENTER FROM RHODOBACTER SPHAEROIDES IN THE CHARGE-NEUTRAL DQAQB STATE WITH THE PROTON TRANSFER INHIBITOR ZN2+'''<br /> | ||
==Overview== | ==Overview== | ||
The reaction center (RC) from Rhodobacter sphaeroides couples light-driven | The reaction center (RC) from Rhodobacter sphaeroides couples light-driven electron transfer to protonation of a bound quinone acceptor molecule, Q(B), within the RC. The binding of Cd(2+) or Zn(2+) has been previously shown to inhibit the rate of reduction and protonation of Q(B). We report here on the metal binding site, determined by x-ray diffraction at 2.5-A resolution, obtained from RC crystals that were soaked in the presence of the metal. The structures were refined to R factors of 23% and 24% for the Cd(2+) and Zn(2+) complexes, respectively. Both metals bind to the same location, coordinating to Asp-H124, His-H126, and His-H128. The rate of electron transfer from Q(A)(-) to Q(B) was measured in the Cd(2+)-soaked crystal and found to be the same as in solution in the presence of Cd(2+). In addition to the changes in the kinetics, a structural effect of Cd(2+) on Glu-H173 was observed. This residue was well resolved in the x-ray structure-i.e., ordered-with Cd(2+) bound to the RC, in contrast to its disordered state in the absence of Cd(2+), which suggests that the mobility of Glu-H173 plays an important role in the rate of reduction of Q(B). The position of the Cd(2+) and Zn(2+) localizes the proton entry into the RC near Asp-H124, His-H126, and His-H128. Based on the location of the metal, likely pathways of proton transfer from the aqueous surface to Q(B) are proposed. | ||
==About this Structure== | ==About this Structure== | ||
1DV6 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 FE2, ZN, CL, BCL, BPH, U10 and LDA as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | 1DV6 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=FE2:'>FE2</scene>, <scene name='pdbligand=ZN:'>ZN</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> 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=1DV6 OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Rhodobacter sphaeroides]] | [[Category: Rhodobacter sphaeroides]] | ||
[[Category: Abresch, E | [[Category: Abresch, E C.]] | ||
[[Category: Axelrod, H | [[Category: Axelrod, H L.]] | ||
[[Category: Feher, G.]] | [[Category: Feher, G.]] | ||
[[Category: Okamura, M | [[Category: Okamura, M Y.]] | ||
[[Category: Paddock, M | [[Category: Paddock, M L.]] | ||
[[Category: BCL]] | [[Category: BCL]] | ||
[[Category: BPH]] | [[Category: BPH]] | ||
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[[Category: x-ray crystallography]] | [[Category: x-ray crystallography]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:20:46 2008'' |