Abstract
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 language | English (US) |
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Pages (from-to) | 509-516 |
Number of pages | 8 |
Journal | Nature Structural Biology |
Volume | 6 |
Issue number | 6 |
DOIs | |
State | Published - 1999 |
Externally published | Yes |
ASJC Scopus subject areas
- Structural Biology
- Biochemistry
- Genetics