The Cu(A) domain of Thermus thermophilus ba3-type cytochrome C oxidase at 1.6 Å resolution

P. A. Williams, N. J. Blackburn, D. Sanders, H. Bellamy, E. A. Stura, J. A. Fee, D. E. McRee

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114 Scopus citations


The structure of the Cu(A)-containing, extracellular domain of Thermus thermophilus ba3-type cytochrome c oxidase has been determined to 1.6 Å resolution using multiple X-ray wavelength anomalous dispersion (MAD). The Cu2S2 cluster forms a planar rhombus with a copper-copper distance of 2.51 ± 0.03 Å. X-ray absorption fine-structure (EXAFS) studies show that this distance is unchanged by crystallization. The Cu(A) center is asymmetrical; one copper is tetrahedrally coordinated to two bridging cysteine thiolates, one histidine nitrogen and one methionine sulfur, while the other is trigonally coordinated by the two cysteine thiolates and a histidine nitrogen. Combined sequence-structure alignment of amino acid sequences reveals conserved interactions between cytochrome c oxidase subunits I and II.

Original languageEnglish (US)
Pages (from-to)509-516
Number of pages8
JournalNature Structural Biology
Issue number6
StatePublished - Jan 1 1999
Externally publishedYes

ASJC Scopus subject areas

  • Structural Biology
  • Biochemistry
  • Genetics


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