标题：Complex of Aspartate Carbamoyltransferase from Escherichia coli with Its Allosteric Inhibitor, Cytidine Triphosphate: Electron Density at 5.9-Å Resolution
期刊名称：Proceedings of the National Academy of Sciences
印刷版ISSN：0027-8424
电子版ISSN：1091-6490
出版年度：1974
卷号：71
期号：11
页码：4437-4441
DOI：10.1073/pnas.71.11.4437
语种：English
出版社：The National Academy of Sciences of the United States of America
摘要：Following our earlier determination of the three-dimensional structure of aspartate carbamoyltransferase (EC 2.1.3.2 ; carbamoylphosphate: L-aspartate carbamoyltransferase) to 5.5-A resolution [S. G. Warren, B. F. P. Edwards, D. R. Evans, D. C. Wiley & W. N. Lipscomb (1973) Proc. Nat. Acad. Sci. USA 70, 1117-1121], we report here, from a different crystal form, the three-dimensional structure at 5.9 A of this enzyme complexed with its allosteric inhibitor, cytidine triphosphate. Location of the major binding site of this inhibitor within each of the six regulatory chains is made secure by comparison of these results with those obtained upon binding of 5-iodocytidine triphosphate to the enzyme. Conformational changes in the aspartate carbamoyltransferase molecule when this inhibitor binds are described briefly at 5.9-A resolution.
关键词：allosteric behavior ; multisubunit enzyme ; mechanism of enzymes ; conformational changes ; protein crystallography
