1A59
COLD-ACTIVE CITRATE SYNTHASE
Summary for 1A59
Entry DOI | 10.2210/pdb1a59/pdb |
Descriptor | CITRATE SYNTHASE, COENZYME A, CITRIC ACID (3 entities in total) |
Functional Keywords | cold-activity |
Biological source | Antarctic bacterium DS2-3R |
Total number of polymer chains | 1 |
Total formula weight | 42708.75 |
Authors | Russell, R.J.M.,Gerike, U.,Danson, M.J.,Hough, D.W.,Taylor, G.L. (deposition date: 1998-02-20, release date: 1999-03-30, Last modification date: 2024-02-07) |
Primary citation | Russell, R.J.,Gerike, U.,Danson, M.J.,Hough, D.W.,Taylor, G.L. Structural adaptations of the cold-active citrate synthase from an Antarctic bacterium. Structure, 6:351-361, 1998 Cited by PubMed Abstract: The structural basis of adaptation of enzymes to low temperature is poorly understood. Dimeric citrate synthase has been used as a model enzyme to study the structural basis of thermostability, the structure of the enzyme from organisms living in habitats at 55 degrees C and 100 degrees C having previously been determined. Here the study is extended to include a citrate synthase from an Antarctic bacterium, allowing us to explore the structural basis of cold activity and thermostability across the whole temperature range over which life is known to exit. PubMed: 9551556DOI: 10.1016/S0969-2126(98)00037-9 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.09 Å) |
Structure validation
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