2CUA

THE CUA DOMAIN OF CYTOCHROME BA3 FROM THERMUS THERMOPHILUS

Summary for 2CUA

• Entry DOI: 10.2210/pdb2cua/pdb
• Descriptor: PROTEIN (CUA), ZINC ION, DINUCLEAR COPPER ION, ... (4 entities in total)
• Functional Keywords: cua center, electron transport
• Biological source: Thermus thermophilus
• Total number of polymer chains: 2
• Total formula weight: 30018.46

Authors

Williams, P.A.,Blackburn, N.J.,Sanders, D.,Bellamy, H.,Stura, E.A.,Fee, J.A.,Mcree, D.E. (deposition date: 1999-02-18, release date: 1999-05-28, Last modification date: 2023-12-27)

Primary citation

Williams, P.A.,Blackburn, N.J.,Sanders, D.,Bellamy, H.,Stura, E.A.,Fee, J.A.,McRee, D.E.
The CuA domain of Thermus thermophilus ba3-type cytochrome c oxidase at 1.6 A resolution.
Nat.Struct.Biol., 6:509-516, 1999

PubMed 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.

PubMed: 10360350
DOI: 10.1038/9274

Experimental method

X-RAY DIFFRACTION (1.6 Å)