1r2c
From Proteopedia
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| , resolution 2.86Å | |||||||
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| Ligands: | , , , , , , , , , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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
Page seeded by OCA on Sun Mar 30 23:22:14 2008
