4R7G

Determination of the formylglycinamide ribonucleotide amidotransferase ammonia pathway by combining 3D-RISM theory with experiment

4R7G の概要

• エントリーDOI: 10.2210/pdb4r7g/pdb
• 関連するPDBエントリー: 1T3t
• 分子名称: Phosphoribosylformylglycinamidine synthase, MAGNESIUM ION, SULFATE ION, ... (5 entities in total)
• 機能のキーワード: gene duplication, amidotransferase, atp binding, ligase
• 由来する生物種: Salmonella typhimurium LT2
• 細胞内の位置: Cytoplasm : P74881
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 143656.93

構造登録者

Tanwar, A.S.,Sindhikara, D.J.,Hirata, F.,Anand, R. (登録日: 2014-08-27, 公開日: 2015-01-21, 最終更新日: 2023-11-08)

主引用文献

Tanwar, A.S.,Sindhikara, D.J.,Hirata, F.,Anand, R.
Determination of the formylglycinamide ribonucleotide amidotransferase ammonia pathway by combining 3D-RISM theory with experiment.
Acs Chem.Biol., 10:698-704, 2015

PubMed Abstract: Molecular tunnels in enzyme systems possess variable architecture and are therefore difficult to predict. In this work, we design and apply an algorithm to resolve the pathway followed by ammonia using the bifunctional enzyme formylglycinamide ribonucleotide amidotransferase (FGAR-AT) as a model system. Though its crystal structure has been determined, an ammonia pathway connecting the glutaminase domain to the 30 Å distal FGAR/ATP binding site remains elusive. Crystallography suggested two purported paths: an N-terminal-adjacent path (path 1) and an auxiliary ADP-adjacent path (path 2). The algorithm presented here, RismPath, which enables fast and accurate determination of solvent distribution inside a protein channel, predicted path 2 as the preferred mode of ammonia transfer. Supporting experimental studies validate the identity of the path, and results lead to the conclusion that the residues in the middle of the channel do not partake in catalytic coupling and serve only as channel walls facilitating ammonia transfer.

PubMed: 25551173
DOI: 10.1021/cb501015r

実験手法

X-RAY DIFFRACTION (2.9 Å)