1dv3

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[[Image:1dv3.gif|left|200px]]<br /><applet load="1dv3" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1dv3.gif|left|200px]]
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caption="1dv3, resolution 2.50&Aring;" />
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'''PHOTOSYNTHETIC REACTION CENTER FROM RHODOBACTER SPHAEROIDES IN THE CHARGE-SEPARATED D+QAQB-STATE WITH THE PROTON TRANSFER INHIBITOR CD2+'''<br />
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{{Structure
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|PDB= 1dv3 |SIZE=350|CAPTION= <scene name='initialview01'>1dv3</scene>, resolution 2.50&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene>, <scene name='pdbligand=CD:CADMIUM+ION'>CD</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=BCL:BACTERIOCHLOROPHYLL+A'>BCL</scene>, <scene name='pdbligand=BPH:BACTERIOPHEOPHYTIN+A'>BPH</scene>, <scene name='pdbligand=U10:UBIQUINONE-10'>U10</scene> and <scene name='pdbligand=LDA:LAURYL DIMETHYLAMINE-N-OXIDE'>LDA</scene>
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|ACTIVITY=
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|GENE=
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}}
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'''PHOTOSYNTHETIC REACTION CENTER FROM RHODOBACTER SPHAEROIDES IN THE CHARGE-SEPARATED D+QAQB-STATE WITH THE PROTON TRANSFER INHIBITOR CD2+'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1DV3 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=CD:'>CD</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=1DV3 OCA].
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1DV3 is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Rhodobacter_sphaeroides Rhodobacter sphaeroides]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DV3 OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10677497 10677497]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/10677497 10677497]
[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Rhodobacter sphaeroides]]
[[Category: Rhodobacter sphaeroides]]
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[[Category: metal ion binding]]
[[Category: metal ion binding]]
[[Category: proton transfer]]
[[Category: proton transfer]]
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[[Category: rhodobacter sphaeroides]]
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[[Category: rhodobacter sphaeroide]]
[[Category: x-ray crystallography]]
[[Category: x-ray crystallography]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:20:54 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:44:49 2008''

Revision as of 08:44, 20 March 2008

Image:1dv3.gif


PDB ID 1dv3

Drag the structure with the mouse to rotate
, resolution 2.50Å
Ligands: , , , , , and
Coordinates: save as pdb, mmCIF, xml



PHOTOSYNTHETIC REACTION CENTER FROM RHODOBACTER SPHAEROIDES IN THE CHARGE-SEPARATED D+QAQB-STATE WITH THE PROTON TRANSFER INHIBITOR CD2+


Overview

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

1DV3 is a Protein complex structure of sequences from Rhodobacter sphaeroides. Full crystallographic information is available from OCA.

Reference

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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