1GK3

Histidine Ammonia-Lyase (HAL) Mutant D145A from Pseudomonas putida

1GK3 の概要

• エントリーDOI: 10.2210/pdb1gk3/pdb
• 関連するPDBエントリー: 1B8F 1EB4 1GK2 1GKJ 1GKM
• 分子名称: HISTIDINE AMMONIA-LYASE, SULFATE ION, GLYCEROL, ... (4 entities in total)
• 機能のキーワード: lyase, ammonia-lyase, histidine degradation
• 由来する生物種: PSEUDOMONAS PUTIDA
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 53799.40

構造登録者

Baedeker, M.,Schulz, G.E. (登録日: 2001-08-07, 公開日: 2002-02-21, 最終更新日: 2024-05-08)

主引用文献

Baedeker, M.,Schulz, G.E.
Autocatalytic Peptide Cyclization During Chain Folding of Histidine Ammonia-Lyase.
Structure, 10:61-67, 2002

PubMed Abstract: Histidine ammonia-lyase requires a 4-methylidene-imidazole-5-one group (MIO) that is produced autocatalytically by a cyclization and dehydration step in a 3-residue loop of the polypeptide. The crystal structures of three mutants have been established. Two mutants were inactive and failed to form MIO, but remained unchanged elsewhere. The third mutant showed very low activity and formed MIO, although it differed from an MIO-less mutant only by an additional 329-C(beta) atom. This atom forms one constraint during MIO formation, the other being the strongly connected Asp145. An exploration of the conformational space of the MIO-forming loop showed that the cyclization is probably enforced by a mechanic compression in a late stage of chain folding and is catalyzed by a well-connected internal water molecule. The cyclization of the respective 3-residue loop of green fluorescent protein is likely to occur in a similar reaction.

PubMed: 11796111
DOI: 10.1016/S0969-2126(01)00692-X

実験手法

X-RAY DIFFRACTION (2.25 Å)