2cua

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2cua, resolution 1.60Å

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THE CUA DOMAIN OF CYTOCHROME BA3 FROM THERMUS THERMOPHILUS

Overview

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.

About this Structure

2CUA is a Single protein structure of sequence from Thermus thermophilus with ZN and CUA as ligands. Active as Cytochrome-c oxidase, with EC number 1.9.3.1 Full crystallographic information is available from OCA.

Reference

The CuA domain of Thermus thermophilus ba3-type cytochrome c oxidase at 1.6 A resolution., Williams PA, Blackburn NJ, Sanders D, Bellamy H, Stura EA, Fee JA, McRee DE, Nat Struct Biol. 1999 Jun;6(6):509-16. PMID:10360350

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