The CuA domain of Thermus thermophilus ba3-type cytochrome c oxidase at 1.6 A resolution

Nat Struct Biol. 1999 Jun;6(6):509-16. doi: 10.1038/9274.

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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Azurin / analogs & derivatives
  • Azurin / chemistry
  • Binding Sites
  • Conserved Sequence
  • Copper / metabolism*
  • Crystallization
  • Crystallography, X-Ray
  • Cysteine / metabolism
  • Cytochrome b Group / chemistry*
  • Cytochrome b Group / metabolism
  • Electron Transport Complex IV / chemistry*
  • Electron Transport Complex IV / metabolism
  • Histidine / metabolism
  • Methionine / metabolism
  • Models, Molecular
  • Molecular Sequence Data
  • Protein Conformation
  • Protein Folding
  • Protein Structure, Secondary
  • Sequence Alignment
  • Sulfur / metabolism
  • Thermus thermophilus / chemistry
  • Thermus thermophilus / enzymology*
  • Zinc / metabolism

Substances

  • Cytochrome b Group
  • cupredoxin
  • Azurin
  • Histidine
  • Sulfur
  • Copper
  • Methionine
  • cytochrome ba3
  • Electron Transport Complex IV
  • Zinc
  • Cysteine

Associated data

  • PDB/2CUA
  • PDB/R2CUASF