| Literature DB >> 10360350 |
P A Williams1, N J Blackburn, D Sanders, H Bellamy, E A Stura, J A Fee, D E McRee.
Abstract
The structure of the CuA-containing, extracellular domain of Thermus thermophilus ba3-type cytochrome c oxidase has been determined to 1.6 A 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 A. X-ray absorption fine-structure (EXAFS) studies show that this distance is unchanged by crystallization. The CuA 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.Entities:
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Year: 1999 PMID： 10360350 DOI： 10.1038/9274
Source DB: PubMed Journal: Nat Struct Biol ISSN： 1072-8368