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. 1974 Nov;71(11):4437–4441. doi: 10.1073/pnas.71.11.4437

Complex of Aspartate Carbamoyltransferase from Escherichia coli with Its Allosteric Inhibitor, Cytidine Triphosphate: Electron Density at 5.9-Å Resolution

Brian F P Edwards 1, David R Evans 1, Stephen G Warren 1, Hugo L Monaco 1, Scott M Landfear 1, George Eisele 1, James L Crawford 1, Don C Wiley 1, William N Lipscomb 1
PMCID: PMC433901  PMID: 4612518

Abstract

Following our earlier determination of the three-dimensional structure of aspartate carbamoyltransferase (EC 2.1.3.2; carbamoylphosphate: L-aspartate carbamoyltransferase) to 5.5-Å 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 Å 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-Å resolution.

Keywords: allosteric behavior, multisubunit enzyme, mechanism of enzymes, conformational changes, protein crystallography

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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