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. 1984 Jul;81(13):4037–4040. doi: 10.1073/pnas.81.13.4037

Structure of unligated aspartate carbamoyltransferase of Escherichia coli at 2.6-A resolution.

H M Ke, R B Honzatko, W N Lipscomb
PMCID: PMC345363  PMID: 6377306

Abstract

The three-dimensional structure of the allosteric enzyme aspartate carbamoyltransferase (EC 2.1.3.2) has been refined to a crystallographic R-factor of 0.24 at 2.6-A resolution in the space group P321, where a and b are 122.1 A and c is 142.2 A. This structure is isomorphous to the form of the enzyme complexed to the allosteric inhibitor cytidine triphosphate. All sources of sequence information have been evaluated against the electron density. The corrected amino acid sequences of the catalytic and regulatory proteins have been incorporated in the model, and three regions in the active site are described: (i) near arginine-105, histidine-134, and arginine-167, (ii) near lysine-232 and arginine-229, and (iii) near lysine-83 and lysine-84.

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Selected References

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

  1. Bethell M. R., Smith K. E., White J. S., Jones M. E. Carbamyl phosphate: an allosteric substrate for aspartate transcarbamylase of Escherichia coli. Proc Natl Acad Sci U S A. 1968 Aug;60(4):1442–1449. doi: 10.1073/pnas.60.4.1442. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. GERHART J. C., PARDEE A. B. ASPARTATE TRANSCARBAMYLASE, AN ENZYME DESIGNED FOR FEEDBACK INHIBITION. Fed Proc. 1964 May-Jun;23:727–735. [PubMed] [Google Scholar]
  3. GERHART J. C., PARDEE A. B. The enzymology of control by feedback inhibition. J Biol Chem. 1962 Mar;237:891–896. [PubMed] [Google Scholar]
  4. Gerhart J. C., Holoubek H. The purification of aspartate transcarbamylase of Escherichia coli and separation of its protein subunits. J Biol Chem. 1967 Jun 25;242(12):2886–2892. [PubMed] [Google Scholar]
  5. Heyde E. A unifying concept for the active site region in aspartate transcarbamylase. Biochim Biophys Acta. 1976 Nov 8;452(1):81–88. doi: 10.1016/0005-2744(76)90059-0. [DOI] [PubMed] [Google Scholar]
  6. Honzatko R. B., Crawford J. L., Monaco H. L., Ladner J. E., Ewards B. F., Evans D. R., Warren S. G., Wiley D. C., Ladner R. C., Lipscomb W. N. Crystal and molecular structures of native and CTP-liganded aspartate carbamoyltransferase from Escherichia coli. J Mol Biol. 1982 Sep 15;160(2):219–263. doi: 10.1016/0022-2836(82)90175-9. [DOI] [PubMed] [Google Scholar]
  7. Honzatko R. B., Lipscomb W. N. Interactions of phosphate ligands with Escherichia coli aspartate carbamoyltransferase in the crystalline state. J Mol Biol. 1982 Sep 15;160(2):265–286. doi: 10.1016/0022-2836(82)90176-0. [DOI] [PubMed] [Google Scholar]
  8. Hoover T. A., Roof W. D., Foltermann K. F., O'Donovan G. A., Bencini D. A., Wild J. R. Nucleotide sequence of the structural gene (pyrB) that encodes the catalytic polypeptide of aspartate transcarbamoylase of Escherichia coli. Proc Natl Acad Sci U S A. 1983 May;80(9):2462–2466. doi: 10.1073/pnas.80.9.2462. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Konigsberg W. H., Henderson L. Amino acid sequence of the catalytic subunit of aspartate transcarbamoylase from Escherichia coli. Proc Natl Acad Sci U S A. 1983 May;80(9):2467–2471. doi: 10.1073/pnas.80.9.2467. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Ladner J. E., Kitchell J. P., Honzatko R. B., Ke H. M., Volz K. W., Kalb A. J., Ladner R. C., Lipscomb W. N. Gross quaternary changes in aspartate carbamoyltransferase are induced by the binding of N-(phosphonacetyl)-L-aspartate: A 3.5-A resolution study. Proc Natl Acad Sci U S A. 1982 May;79(10):3125–3128. doi: 10.1073/pnas.79.10.3125. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Lauritzen A. M., Lipscomb W. N. Modification of three active site lysine residues in the catalytic subunit of aspartate transcarbamylase by D- and L-bromosuccinate. J Biol Chem. 1982 Feb 10;257(3):1312–1319. [PubMed] [Google Scholar]
  12. Schachman H. K., Pauza C. D., Navre M., Karels M. J., Wu L., Yang Y. R. Location of amino acid alterations in mutants of aspartate transcarbamoylase: Structural aspects of interallelic complementation. Proc Natl Acad Sci U S A. 1984 Jan;81(1):115–119. doi: 10.1073/pnas.81.1.115. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Weber K. New structural model of E. coli aspartate transcarbamylase and the amino-acid sequence of the regulatory polypeptide chain. Nature. 1968 Jun 22;218(5147):1116–1119. doi: 10.1038/2181116a0. [DOI] [PubMed] [Google Scholar]
  14. Wiley D. C., Evans D. R., Warren S. G., McMurray C. H., Edwards B. F., Franks W. A., Lipscomb W. N. The 5.5 Angstrom resolution structure of the regulatory enzyme, asparate transcarbamylase. Cold Spring Harb Symp Quant Biol. 1972;36:285–290. doi: 10.1101/sqb.1972.036.01.038. [DOI] [PubMed] [Google Scholar]
  15. Wiley D. C., Lipscomb W. N. Crystallographic determination of symmetry of aspartate transcarbamylase. Nature. 1968 Jun 22;218(5147):1119–1121. doi: 10.1038/2181119a0. [DOI] [PubMed] [Google Scholar]

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