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- W1977839951 abstract "Abstract The three‐dimensional structure of the multisubunit allosteric enzyme, aspartate transcarbamylase, has been determined to 5.5 Å resolution. An unusual feature of the molecule is a large central aqueous cavity 50 Å × 50 Å × 25 Å, into which the active sites face. Access to the central cavity and the active site region is provided by six equivalent channels of 15 Å diameter. A complex C 6 R 4 , composed of catalytic trimers C 3 and of regulatory dimers R 2 , has been isolated upon treatment of aspartate transcarbamylase (ATCase, C 6 R 6 ) by mercurials. The specific catalytic activity of C 6 R 4 is essentially the same as that of ATCase, about 70% of that of the catalytic trimers at 30 mM aspartate and saturating carbamyl phosphate. Allosteric interactions are reduced in C 6 R 4 as compared with those in ATCase. In the homotropic interactions the Hill coefficient is reduced from approximately 3.3 to 2.1 at pH 8.3, while the heterotropic interactions of both cytidine triphosphate (CTP) and adenosine triphosphate (ATP) are reduced substantially but not abolished at pH 8.3. Thus, the allosteric transitions involved in the regulatory mechanisms do not require the intact structure C 6 R 6 . Also, this regulation is not simply the control of access of substrates or products to or from the large central aqueous cavity in the ATCase molecule. Comparison of electron density maps at 5.5 Å resolution for ATCase and for the complex of ATCase with CTP shows substantial similarities throughout the three‐dimensional electron density maps. Significant differences are seen, however, in the region of the regulatory dimers R 2 where CTP adds, and near the active sites in the catalytic trimers C 3 ." @default.
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- W1977839951 date "1974-01-01" @default.
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- W1977839951 title "Three-dimensional structures at 5.5 Å resolution and regulatory processes in aspartate transcarbamylase from E. coli" @default.
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- W1977839951 doi "https://doi.org/10.1002/jss.400020203" @default.
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