Structural basis for ordered substrate binding and cooperativity in aspartate transcarbamoylase. | Proc Natl Acad Sci U S A;102(25): 8881-6, 2005 Jun 21. | MEDLINE

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Structural basis for ordered substrate binding and cooperativity in aspartate transcarbamoylase.

Wang, Jie; Stieglitz, Kimberly A; Cardia, James P; Kantrowitz, Evan R.

Affiliation

Wang J; Department of Chemistry, Boston College, Merkert Chemistry Center, Chestnut Hill, MA 02467, USA.

Proc Natl Acad Sci U S A ; 102(25): 8881-6, 2005 Jun 21.

Article in En | MEDLINE | ID: mdl-15951418

Subject(s)

Aspartate Carbamoyltransferase/chemistry; Aspartate Carbamoyltransferase/metabolism; Allosteric Regulation; Amino Acid Sequence; Binding Sites; Crystallography, X-Ray; Escherichia coli/enzymology; Models, Molecular; Protein Conformation; Static Electricity

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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Aspartate Carbamoyltransferase Language: En Journal: Proc Natl Acad Sci U S A Year: 2005 Type: Article Affiliation country: United States

Search on Google

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Aspartate Carbamoyltransferase Language: En Journal: Proc Natl Acad Sci U S A Year: 2005 Type: Article Affiliation country: United States