Atomic structure of the actin: DNase I complex

• Published in: Nature (London) Vol. 347; no. 6288; pp. 37 - 44
• Main Authors: Kabsch, Wolfgang, Mannherz, Hans Georg, Suck, Dietrich, Pai, Emil F, Holmes, Kenneth C
• Format: Journal Article
• Language: English
• Published: London Nature Publishing 06.09.1990; Nature Publishing Group
• Subjects: Actin; Actins - metabolism; Adenosine diphosphate; Adenosine Diphosphate - metabolism; Adenosine Triphosphate - metabolism; Amino Acid Sequence; Amino acids; Animals; Atomic structure; ATP; Binding Sites; Biochemistry; Biological and medical sciences; Calcium - metabolism; Cattle; Cellular biology; Chemical Phenomena; Chemistry, Physical; Conformation; Control systems; Cytoskeleton; Deoxyribonuclease; deoxyribonuclease I; Deoxyribonuclease I - metabolism; Fundamental and applied biological sciences. Psychology; Gene duplication; Hexokinase; Interactions. Associations; Intermolecular phenomena; Molecular biophysics; Molecular Structure; Molecules; Muscles; Muscles - analysis; Musculoskeletal system; Myosins - metabolism; Pancreas - enzymology; Phosphates; Polypeptides; Protein Conformation; Proteins; Proteolysis; Rabbits; Residues; Rotation; Topology; X-Ray Diffraction; Bovine; Calcium; Enzyme; Actins; Rabbit; Contractile protein; Molecular interaction; Lagomorpha; ADP; X ray diffraction; Vertebrata; Mammalia; Deoxyribonuclease I; Molecular model; Artiodactyla; ATP; Ungulata
• ISSN: 0028-0836; 1476-4687
• DOI: 10.1038/347037a0

The atomic models of the complex between rabbit skeletal muscle actin and bovine pancreatic deoxyribonuclease I both in the ATP and ADP forms have been determined by X-ray analysis at an effective resolution of 2.8 A and 3A, respectively. The two structures are very similar. The actin molecule consists of two domains which can be further subdivided into two subdomains. ADP or ATP is located in the cleft between the domains with a calcium ion bound to the beta- or beta- and gamma-phosphates, respectively. The motif of a five-stranded beta sheet consisting of a beta meander and a right handed beta alpha beta unit appears in each domain suggesting that gene duplication might have occurred. These sheets have the same topology as that found in hexokinase.