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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Gouaux, J. E. Lipscomb, W. N. |
| Description | Author Affiliation: Gouaux JE ( Gibbs Chemical Laboratory, Harvard University, Cambridge, MA 02138.); |
| Abstract | Screened precession x-ray photographs of crystals of native aspartate carbamoyltransferase (EC 2.1.3.2, from Escherichia coli) ligated with L-aspartate and phosphate reveal the presence of a crystal unit-cell dimension that is intermediate between the T (tense) and R (relaxed) states. Characterizing the intermediate (I) crystal is a c-axis unit-cell dimension of 149 A, halfway between the c-axis length of the T (c = 142 A) and R (c = 156 A) states, in the space group P321. Preservation of the P321 space group indicates that the intermediate crystal form retains a threefold axis of symmetry, and therefore the enzyme has at minimum a threefold axis; however, we do not know whether the molecular twofold axis is conserved. The I crystals are formed by soaking T-state crystals with L-aspartate and phosphate. By raising the concentration of L-aspartate we can further transform the I crystals, without fragmentation, to a form that has the same unit-cell dimensions as R-state crystals grown in the presence of N-(phosphonoacetyl)-L-aspartate. |
| ISSN | 00278424 |
| e-ISSN | 10916490 |
| Journal | Proceedings of the National Academy of Sciences of the United States of America |
| Issue Number | 3 |
| Volume Number | 86 |
| Language | English |
| Publisher | National Academy of Sciences |
| Publisher Date | 1989-03-01 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Aspartate Carbamoyltransferase Metabolism Crystallization Escherichia Coli Enzymology Macromolecular Substances Models, Molecular Models, Theoretical Protein Conformation X-Ray Diffraction Research Support, U.S. Gov't, P.H.S. Multidisciplinary |
| Content Type | Text |
| Resource Type | Article |
| Subject | Multidisciplinary |
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