Structure of the reaction center from Rhodobacter sphaeroides R-26: the protein subunits
Abstract
The three-dimensional structure of the protein subunits of the reaction center (RC) of Rhodobacter sphaeroides has been determined by x-ray diffraction at a resolution of 2.8 Å with an R factor of 26%. The L and M subunits each contain five transmembrane helices and several helices that do not span the membrane. The L and M subunits are related to each other by a 2-fold rotational symmetry axis that is approximately the same as that determined for the cofactors. The H subunit has one transmembrane helix and a globular domain on the cytoplasmic side, which contains a helix that does not span the membrane and several β-sheets. The structural homology with RCs from other purple bacteria is discussed. A structure of the complex formed between the water soluble cytochrome c_2 and the RC from Rb. sphaeroides is proposed.
Additional Information
© 1987 National Academy of Sciences. Contributed by G. Feher. May 18. 1987. We thank E. Abresch for the preparation of the RCs. This work was supported by grants from the National Institutes of Health (AM36053, GM13191, GM31299, and GM07185), the National Science Foundation (DMB85-18922J, a Presidential Young Investigators Award, and the Chicago Community Trust/Searle Scholars Program. The publication costs of this article were defrayed in part by page charge payment. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. §1734 solely to indicate this fact.Attached Files
Published - 34_allen_1987.pdf
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Additional details
- PMCID
- PMC299029
- Eprint ID
- 54548
- Resolver ID
- CaltechAUTHORS:20150209-104007322
- NIH
- AM36053
- NIH
- GM13191
- NIH
- GM31299
- NIH
- GM07185
- NSF
- DMB85-18922
- Chicago Community Trust
- Searle Scholars Program
- Created
-
2015-02-09Created from EPrint's datestamp field
- Updated
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2019-10-03Created from EPrint's last_modified field