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Three-dimensional structure of the complex between the mitochondrial matrix adenylate kinase and its substrate AMP

Journal Article · · Biochemistry; (USA)
OSTI ID:5869119
;  [1]
  1. Institut fuer Organische Chemie und Biochemie der Universitaet, Albertstrasse (West Germany)

Crystals of adenylate kinase from beef heart mitochondrial matrix (EC 2.7.4.10) complexed with its substrate AMP were analyzed by X-ray diffraction. The crystal structure was solved by multiple isomorphous replacement and solvent flattening at a resolution of 3.0 {angstrom}. There are two enzyme-substrate molecules in the asymmetric unit. The resolution was extended to 1.9 {angstrom} by model building and refinement using simulated annealing. The current R-factor is 28.4%. The model is given as a backbone tracing for residues 5-218. The enzyme can be subdivided into three domains, the relative arrangements of which differ slightly but significantly between the two crystallographically independent molecules. When compared with other adenylate kinase structures, the chain fold is similar but the observed domain arrangement differs grossly, suggesting that large parts of the enzyme move during catalysis. The observed binding site of AMP is described. Its location in conjunction with data from homologous proteins clarifies the nucleotide-binding sites of the adenylate kinases. Previous assignments of these sites derived from X-ray crystallographic and nuclear magnetic resonance analyses are discussed.

OSTI ID:
5869119
Journal Information:
Biochemistry; (USA), Journal Name: Biochemistry; (USA) Vol. 29:35; ISSN 0006-2960; ISSN BICHA
Country of Publication:
United States
Language:
English