Crystal structure of the cytochrome bc1 complex from bovine heart mitochondria

Di Xia, Chang An Yu, Hoeon Kim, Jia Zhi Xia, Anatoly M. Kachurin, Li Zhang, Linda Yu, Johann Deisenhofer

Research output: Contribution to journalArticle

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Abstract

On the basis of x-ray diffraction data to a resolution of 2.9 angstroms, atomic models of most protein components of the bovine cytochrome bc1 complex were built, including core 1, core 2, cytochrome b, subunit 6, subunit 7, a carboxyl-terminal fragment of cytochrome c1, and an amino- terminal fragment of the iron-sulfur protein. The positions of the four iron centers within the bc1 complex and the binding sites of the two specific respiratory inhibitors antimycin A and myxothiazol were identified. The membrane-spanning region of each bc1 complex monomer consists of 13 transmembrane helices, eight of which belong to cytochrome b. Closely interacting monomers are arranged as symmetric dimers and form cavities through which the inhibitor binding pockets can be accessed. The proteins core 1 and core 2 are structurally similar to each other and consist of two domains of roughly equal size and identical folding topology.

Original languageEnglish (US)
Pages (from-to)60-66
Number of pages7
JournalScience
Volume277
Issue number5322
DOIs
StatePublished - Jul 4 1997

ASJC Scopus subject areas

  • General

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