1r2c

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(New page: 200px<br /><applet load="1r2c" size="450" color="white" frame="true" align="right" spinBox="true" caption="1r2c, resolution 2.86&Aring;" /> '''PHOTOSYNTHETIC REACT...)
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[[Image:1r2c.gif|left|200px]]<br /><applet load="1r2c" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1r2c, resolution 2.86&Aring;" />
caption="1r2c, resolution 2.86&Aring;" />
'''PHOTOSYNTHETIC REACTION CENTER BLASTOCHLORIS VIRIDIS (ATCC)'''<br />
'''PHOTOSYNTHETIC REACTION CENTER BLASTOCHLORIS VIRIDIS (ATCC)'''<br />
==Overview==
==Overview==
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Light-induced structural changes in the bacterial reaction center were, studied by a time-resolved crystallographic experiment. Crystals of, protein from Blastochloris viridis (formerly Rhodopseudomonas viridis), were reconstituted with ubiquinone and analyzed by monochromatic and Laue, diffraction, in the dark and 3 ms after illuminating the crystal with a, pulsed laser (630 nm, 3 mJ/pulse, 7 ns duration). Refinement of, monochromatic data shows that ubiquinone binds only in the "proximal" Q(B), binding site. No significant structural difference was observed between, the light and dark datasets; in particular, no quinone motion was, detected. This result may be reconciled with previous studies by, postulating equilibration of the "distal" and "proximal" binding sites, upon extended dark adaption, and in which movement of ubiquinone is not, the conformational gate for the first electron transfer between Q(A) and, Q(B).
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Light-induced structural changes in the bacterial reaction center were studied by a time-resolved crystallographic experiment. Crystals of protein from Blastochloris viridis (formerly Rhodopseudomonas viridis) were reconstituted with ubiquinone and analyzed by monochromatic and Laue diffraction, in the dark and 3 ms after illuminating the crystal with a pulsed laser (630 nm, 3 mJ/pulse, 7 ns duration). Refinement of monochromatic data shows that ubiquinone binds only in the "proximal" Q(B) binding site. No significant structural difference was observed between the light and dark datasets; in particular, no quinone motion was detected. This result may be reconciled with previous studies by postulating equilibration of the "distal" and "proximal" binding sites upon extended dark adaption, and in which movement of ubiquinone is not the conformational gate for the first electron transfer between Q(A) and Q(B).
==About this Structure==
==About this Structure==
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1R2C 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, HEM, BCB, BPB, MQ7, UQ2, NS5 and LDA as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1R2C OCA].
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1R2C 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=HEM:'>HEM</scene>, <scene name='pdbligand=BCB:'>BCB</scene>, <scene name='pdbligand=BPB:'>BPB</scene>, <scene name='pdbligand=MQ7:'>MQ7</scene>, <scene name='pdbligand=UQ2:'>UQ2</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=1R2C OCA].
==Reference==
==Reference==
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[[Category: Blastochloris viridis]]
[[Category: Blastochloris viridis]]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: Baxter, R.H.]]
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[[Category: Baxter, R H.]]
[[Category: Moffat, K.]]
[[Category: Moffat, K.]]
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[[Category: Norris, J.R.]]
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[[Category: Norris, J R.]]
[[Category: Pahl, R.]]
[[Category: Pahl, R.]]
[[Category: Ponomarenko, N.]]
[[Category: Ponomarenko, N.]]
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[[Category: secondary quinone (qb)]]
[[Category: secondary quinone (qb)]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 01:13:13 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:46:16 2008''

Revision as of 12:46, 21 February 2008


1r2c, resolution 2.86Å

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PHOTOSYNTHETIC REACTION CENTER BLASTOCHLORIS VIRIDIS (ATCC)

Overview

Light-induced structural changes in the bacterial reaction center were studied by a time-resolved crystallographic experiment. Crystals of protein from Blastochloris viridis (formerly Rhodopseudomonas viridis) were reconstituted with ubiquinone and analyzed by monochromatic and Laue diffraction, in the dark and 3 ms after illuminating the crystal with a pulsed laser (630 nm, 3 mJ/pulse, 7 ns duration). Refinement of monochromatic data shows that ubiquinone binds only in the "proximal" Q(B) binding site. No significant structural difference was observed between the light and dark datasets; in particular, no quinone motion was detected. This result may be reconciled with previous studies by postulating equilibration of the "distal" and "proximal" binding sites upon extended dark adaption, and in which movement of ubiquinone is not the conformational gate for the first electron transfer between Q(A) and Q(B).

About this Structure

1R2C is a Protein complex structure of sequences from Blastochloris viridis with , , , , , , , and as ligands. Full crystallographic information is available from OCA.

Reference

Time-resolved crystallographic studies of light-induced structural changes in the photosynthetic reaction center., Baxter RH, Ponomarenko N, Srajer V, Pahl R, Moffat K, Norris JR, Proc Natl Acad Sci U S A. 2004 Apr 20;101(16):5982-7. Epub 2004 Apr 8. PMID:15073325

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