1B0A

5,10, METHYLENE-TETRAHYDROPHOLATE DEHYDROGENASE/CYCLOHYDROLASE FROM E COLI.

1B0A の概要

• エントリーDOI: 10.2210/pdb1b0a/pdb
• 分子名称: PROTEIN (FOLD BIFUNCTIONAL PROTEIN) (2 entities in total)
• 機能のキーワード: folate, dehydrogenase, cyclcohydrolase, bifunctional, channeling, oxidoreductase, hydrolase
• 由来する生物種: Escherichia coli K12
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 31078.67

構造登録者

Shen, B.W.,Dyer, D.,Huang, J.-Y.,D'Ari, L.,Rabinowitz, J.,Stoddard, B.L. (登録日: 1998-11-06, 公開日: 1999-06-29, 最終更新日: 2023-12-27)

主引用文献

Shen, B.W.,Dyer, D.H.,Huang, J.Y.,D'Ari, L.,Rabinowitz, J.,Stoddard, B.L.
The crystal structure of a bacterial, bifunctional 5,10 methylene-tetrahydrofolate dehydrogenase/cyclohydrolase.
Protein Sci., 8:1342-1349, 1999

PubMed Abstract: The structure of a bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/cyclohydrolase from Escherichia coli has been determined at 2.5 A resolution in the absence of bound substrates and compared to the NADP-bound structure of the homologous enzyme domains from a trifunctional human synthetase enzyme. Superposition of these structures allows the identification of a highly conserved cluster of basic residues that are appropriately positioned to serve as a binding site for the poly-gamma-glutamyl tail of the tetrahydrofolate substrate. Modeling studies and molecular dynamic simulations of bound methylene-tetrahydrofolate and NADP shows that this binding site would allow interaction of the nicotinamide and pterin rings in the dehydrogenase active site. Comparison of these enzymes also indicates differences between their active sites that might allow the development of inhibitors specific to the bacterial target.

PubMed: 10386884

実験手法

X-RAY DIFFRACTION (2.56 Å)