1RLT

Transition State Analogue of ybiV from E. coli K12

1RLT の概要

• エントリーDOI: 10.2210/pdb1rlt/pdb
• 関連するPDBエントリー: 1RLM 1RLO
• 分子名称: Phosphatase, MAGNESIUM ION, ACETATE ION, ... (6 entities in total)
• 機能のキーワード: had family, transition-state analogue, aluminum fluoride, phosphatase, hydrolase
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 122711.88

構造登録者

Roberts, A.,Lee, S.Y.,McCullagh, E.,Silversmith, R.E.,Wemmer, D.E. (登録日: 2003-11-26, 公開日: 2004-12-07, 最終更新日: 2024-12-25)

主引用文献

Roberts, A.,Lee, S.Y.,McCullagh, E.,Silversmith, R.E.,Wemmer, D.E.
Ybiv from Escherichia coli K12 is a HAD phosphatase.
Proteins, 58:790-801, 2005

PubMed Abstract: The protein YbiV from Escherichia coli K12 MG1655 is a hypothetical protein with sequence homology to the haloacid dehalogenase (HAD) superfamily of proteins. Although numerous members of this family have been identified, the functions of few are known. Using the crystal structure, sequence analysis, and biochemical assays, we have characterized YbiV as a HAD phosphatase. The crystal structure of YbiV reveals a two-domain protein, one with the characteristic HAD hydrolase fold, the other an inserted alpha/beta fold. In an effort to understand the mechanism, we also solved and report the structures of YbiV in complex with beryllofluoride (BeF3-) and aluminum trifluoride (AlF3), which have been shown to mimic the phosphorylated intermediate and transition state for hydrolysis, respectively, in analogy to other HAD phosphatases. Analysis of the structures reveals the substrate-binding cavity, which is hydrophilic in nature. Both structure and sequence homology indicate YbiV may be a sugar phosphatase, which is supported by biochemical assays that measured the release of free phosphate on a number of sugar-like substrates. We also investigated available genomic and functional data in an effort to determine the physiological substrate.

PubMed: 15657928
DOI: 10.1002/prot.20267

実験手法

X-RAY DIFFRACTION (2.2 Å)