2AIR

T-state Active Site of Aspartate Transcarbamylase:Crystal Structure of the Carbamyl Phosphate and L-alanosine Ligated Enzyme

2AIR の概要

• エントリーDOI: 10.2210/pdb2air/pdb
• 分子名称: Aspartate carbamoyltransferase catalytic chain, Aspartate carbamoyltransferase regulatory chain, PHOSPHORIC ACID MONO(FORMAMIDE)ESTER, ... (6 entities in total)
• 機能のキーワード: aspartate transcarbamylase, alanosine, carbamyl phosphate, t-state, transferase
• 由来する生物種: Escherichia coli; 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 103672.53

構造登録者

Huang, J.,Lipscomb, W.N. (登録日: 2005-07-30, 公開日: 2006-01-24, 最終更新日: 2023-08-23)

主引用文献

Huang, J.,Lipscomb, W.N.
T-State Active Site of Aspartate Transcarbamylase: Crystal Structure of the Carbamyl Phosphate and l-Alanosine Ligated Enzyme
Biochemistry, 45:346-352, 2006

PubMed Abstract: An X-ray diffraction study to 2.0 A resolution shows that this enzyme, ATCase, is in the T-state (the c3 to c3 distance is 45.2 A) when ATCase is bound to carbamyl phosphate (CP) and to L-alanosine (an analogue of aspartate). This result strongly supports the kinetic results that alanosine did not inhibit the carbamylation of aspartate in the normal reaction of native ATCase plus CP and aspartate [Baillon, J., Tauc, P., and Hervé, G. (1985) Biochemistry 24, 7182-7187]. The structure further reveals that the phosphate of CP is 4 A away from its known position in the R-state and is in the T-state position of P(i) in a recent study of ATCase complexed with products, phosphate (P(i)) and N-carbamyl-L-aspartate [Huang, J., and Lipscomb, W. N. (2004) Biochemistry 43, 6422-6426]. Moreover, the alanosine position in this T-state is somewhat displaced from that expected for its analogue, aspartate, from the R-state position. The relations of these structural aspects to the kinetics are presented.

PubMed: 16401065
DOI: 10.1021/bi051543u

実験手法

X-RAY DIFFRACTION (2 Å)