The CuA domain of Thermus thermophilus ba3-type cytochrome c oxidase at 1.6 A resolution
| Autor: | P A, Williams, N J, Blackburn, D, Sanders, H, Bellamy, E A, Stura, J A, Fee, D E, McRee |
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| Rok vydání: | 1999 |
| Předmět: |
Models
Molecular Protein Folding Binding Sites Protein Conformation Thermus thermophilus Molecular Sequence Data Crystallography X-Ray Cytochrome b Group Protein Structure Secondary Electron Transport Complex IV Zinc Methionine Azurin Histidine Amino Acid Sequence Cysteine Crystallization Sequence Alignment Conserved Sequence Copper Sulfur |
| Zdroj: | Nature structural biology. 6(6) |
| ISSN: | 1072-8368 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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