1YIZ

Aedes aegypti kynurenine aminotrasferase

1YIZ の概要

• エントリーDOI: 10.2210/pdb1yiz/pdb
• 関連するPDBエントリー: 1YIY
• 分子名称: kynurenine aminotransferase; glutamine transaminase, BROMIDE ION (3 entities in total)
• 機能のキーワード: kynurenine, kynurenic acid, kynurenine aminotransferase, aedes, mosquito, plp-enzyme, pyridoxal phosphate, plp, transferase
• 由来する生物種: Aedes aegypti (yellow fever mosquito)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 97528.03

構造登録者

Han, Q.,Gao, Y.G.,Robinson, H.,Ding, H.,Wilson, S.,Li, J. (登録日: 2005-01-13, 公開日: 2005-05-10, 最終更新日: 2024-04-03)

主引用文献

Han, Q.,Gao, Y.G.,Robinson, H.,Ding, H.,Wilson, S.,Li, J.
Crystal structures of Aedes aegypti kynurenine aminotransferase.
FEBS J., 272:2198-2206, 2005

PubMed Abstract: Aedes aegypti kynurenine aminotransferase (AeKAT) catalyzes the irreversible transamination of kynurenine to kynurenic acid, the natural antagonist of NMDA and 7-nicotinic acetycholine receptors. Here, we report the crystal structure of AeKAT in its PMP and PLP forms at 1.90 and 1.55 A, respectively. The structure was solved by a combination of single-wavelength anomalous dispersion and molecular replacement approaches. The initial search model in the molecular replacement method was built with the result of single-wavelength anomalous dispersion data from the Br-AeKAT crystal in combination with homology modeling. The solved structure shows that the enzyme is a homodimer, and that the two subunits are stabilized by a number of hydrogen bonds, salts bridges, and hydrophobic interactions. Each subunit is divided into an N-terminal arm and small and large domains. Based on its folding, the enzyme belongs to the prototypical fold type, aminotransferase subgroup I. The three-dimensional structure shows a strictly conserved 'PLP-phosphate binding cup' featuring PLP-dependent enzymes. The interaction between Cys284 (A) and Cys284 (B) is unique in AeKAT, which might explain the cysteine effect of AeKAT activity. Further mutation experiments of this residue are needed to eventually understand the mechanism of the enzyme modulation by cysteine.

PubMed: 15853804
DOI: 10.1111/j.1742-4658.2005.04643.x

実験手法

X-RAY DIFFRACTION (1.55 Å)