Structure of unligated aspartate carbamoyltransfer...[Proc Natl Acad Sci U S A. 1984] - PubMed Result

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1: Proc Natl Acad Sci U S A. 1984 Jul;81(13):4037-40. Links

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

Ke HM, Honzatko RB, Lipscomb WN.

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.

PMID: 6377306 [PubMed - indexed for MEDLINE]

PMCID: PMC345363

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Structures reported by this article

Crystal Structures Of Aspartate Carbamoyltransferase Ligated With Phosphonoacetamide, Malonate, And Ctp Or Atp At 2.8-Angstroms Resolution And Neutral PH

PDB: 7AT1

Source: Escherichia coli

Method: X-Ray Diffraction | Resolution: 2.8 Å
» See all 9 structures...

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