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

Author:

Roszak Aleksander W.12,Howard Tina D.12,Southall June12,Gardiner Alastair T.12,Law Christopher J.12,Isaacs Neil W.12,Cogdell Richard J.12

Affiliation:

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

Abstract

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 α- and β-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 α-apoproteins. This break, located next to the binding site in the reaction center for the secondary electron acceptor ubiquinone (UQ B ), may provide a portal through which UQ B can transfer electrons to cytochrome b/c 1 .

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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