1ds8: Difference between revisions
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|PDB= 1ds8 |SIZE=350|CAPTION= <scene name='initialview01'>1ds8</scene>, resolution 2.50Å | |PDB= 1ds8 |SIZE=350|CAPTION= <scene name='initialview01'>1ds8</scene>, resolution 2.50Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand= | |LIGAND= <scene name='pdbligand=BCL:BACTERIOCHLOROPHYLL+A'>BCL</scene>, <scene name='pdbligand=BPH:BACTERIOPHEOPHYTIN+A'>BPH</scene>, <scene name='pdbligand=CD:CADMIUM+ION'>CD</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene>, <scene name='pdbligand=LDA:LAURYL+DIMETHYLAMINE-N-OXIDE'>LDA</scene>, <scene name='pdbligand=U10:UBIQUINONE-10'>U10</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY=[[1aig|1aig]], [[1aij|1AIJ]], [[1dv3|1DV3]], [[1dv6|1DV6]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ds8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ds8 OCA], [http://www.ebi.ac.uk/pdbsum/1ds8 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ds8 RCSB]</span> | |||
}} | }} | ||
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[[Category: Okamura, M Y.]] | [[Category: Okamura, M Y.]] | ||
[[Category: Paddock, M L.]] | [[Category: Paddock, M L.]] | ||
[[Category: bacterial photosynthesis]] | [[Category: bacterial photosynthesis]] | ||
[[Category: cation binding]] | [[Category: cation binding]] | ||
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[[Category: x-ray crystallography]] | [[Category: x-ray crystallography]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:47:37 2008'' |
Revision as of 19:47, 30 March 2008
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, resolution 2.50Å | |||||||
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Ligands: | , , , , , , | ||||||
Related: | 1aig, 1AIJ, 1DV3, 1DV6
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Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
Coordinates: | save as pdb, mmCIF, xml |
PHOTOSYNTHETIC REACTION CENTER FROM RHODOBACTER SPHAEROIDES IN THE CHARGE-NEUTRAL DQAQB STATE WITH THE PROTON TRANSFER INHIBITOR CD2+
OverviewOverview
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 StructureAbout this Structure
1DS8 is a Protein complex structure of sequences from Rhodobacter sphaeroides. Full crystallographic information is available from OCA.
ReferenceReference
Determination of the binding sites of the proton transfer inhibitors Cd2+ and Zn2+ in bacterial reaction centers., Axelrod HL, Abresch EC, Paddock ML, Okamura MY, Feher G, Proc Natl Acad Sci U S A. 2000 Feb 15;97(4):1542-7. PMID:10677497
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