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Science 12 December 2003:
Vol. 302. no. 5652, pp. 1969 - 1972
DOI: 10.1126/science.1088892
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Reports

Crystal Structure of the RC-LH1 Core Complex from Rhodopseudomonas palustris

Aleksander W. Roszak,1 Tina D. Howard,2 June Southall,2 Alastair T. Gardiner,2 Christopher J. Law,2 Neil W. Isaacs,1* Richard J. Cogdell2*

The crystal structure at 4.8 angstrom resolution of the reaction center–light harvesting 1 (RC–LH1) core complex from Rhodopseudomonas palustris shows the reaction center surrounded by an oval LH1 complex that consists of 15 pairs of transmembrane helical {alpha}- and ß-apoproteins and their coordinated bacteriochlorophylls. Complete closure of the RC by the LH1 is prevented by a single transmembrane helix, out of register with the array of inner LH1 {alpha}-apoproteins. This break, located next to the binding site in the reaction center for the secondary electron acceptor ubiquinone (UQB), may provide a portal through which UQB can transfer electrons to cytochrome b/c1.

1 Department of Chemistry, Institute of Biomedical and Life Sciences, University of Glasgow, Glasgow G12 8QQ, UK
2 Division of Biochemistry and Molecular Biology, Institute of Biomedical and Life Sciences, University of Glasgow, Glasgow G12 8QQ, UK

* To whom correspondence should be addressed. Email: r.cogdell{at}bio.gla.ac.uk (R.J.C.) or n.isaacs{at}chem.gla.ac.uk (N.W.I.)

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