Crystallization and preliminary X-ray analysis of pyruvate kinase from Bacillus stearothermophilus
- Department of Food and Nutritional Sciences, University of Shizuoka, Yada 52-1, Shizuoka 422-8526 (Japan)
This report describes the crystallization and X-ray diffraction data collection of three types (wild-type, W416F/V435W and C9S/C268S) of B. stearothermophilus. Crystals of C9S/C268S belonged to space group P6{sub 2}22 and diffracted to a resolution of 2.4 Å. Pyruvate kinase (PK) from a moderate thermophile, Bacillus stearothermophilus (BstPK), is an allosteric enzyme activated by AMP and ribose 5-phosphate but not by fructose 1,6-bisphosphate (FBP). However, almost all other PKs are activated by FBP. The wild-type and W416F/V435W mutant BstPKs were crystallized by the hanging-drop vapour-diffusion method. However, they were unsuitable for structural analysis because their data sets exhibited low completeness. A crystal suitable for structural analysis was obtained using C9S/C268S enzyme. The crystal belonged to space group P6{sub 2}22, with unit-cell parameters a = b = 145.97, c = 118.03 Å.
- OSTI ID:
- 22356047
- Journal Information:
- Acta Crystallographica. Section F, Vol. 61, Issue Pt 8; Other Information: PMCID: PMC1952353; PMID: 16511150; PUBLISHER-ID: za5104; OAI: oai:pubmedcentral.nih.gov:1952353; Copyright (c) International Union of Crystallography 2005; Country of input: International Atomic Energy Agency (IAEA); ISSN 1744-3091
- Country of Publication:
- United Kingdom
- Language:
- English
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