Three-dimensional structure of cat muscle pyruvate kinase at 3-1 A resolution.

Journal article

X-ray diffraction data sets have been collected by screened precession photography to a nominal resolution of 3·1 Å from crystals of cat muscle pyruvate kinase. The films were processed using an Optronics film scanner and phase angles were estimated by the method of single isomorphous replacement with anomalous scattering measurements. The data have been combined with the 6 Å diffractometer data (Stammers and Muirhead, 1975) and a Fourier map calculated. The map shows the presence of a large amount of regular secondary structure, mainly parallel β-sheet interconnected by α-helices. Each subunit is folded into three domains two of which have a central core of β-sheet. The active site is situated at the carboxyl end of one of these sheet regions. © 1977.

Authors: Stammers, D; Muirhead, H

• Publication status: Published
• Journal: Journal of molecular biology
• Volume: 112
• Issue: 2
• Pages: 309-316
• Publication date: 1977-05-01
• DOI: 10.1016/s0022-2836(77)80146-0
• EISSN: 1089-8638
• ISSN: 0022-2836
• Language: English
• Keywords: Animals; Pyruvate Kinase; X-Ray Diffraction; Muscles; Models, Molecular; Cats; Protein Conformation