1M33

Crystal Structure of BioH at 1.7 A

1M33 の概要

• エントリーDOI: 10.2210/pdb1m33/pdb
• 分子名称: BioH protein, 3-HYDROXY-PROPANOIC ACID, 1,2-ETHANEDIOL, ... (4 entities in total)
• 機能のキーワード: alpha-betta-alpha sandwich, structural genomics, psi, protein structure initiative, midwest center for structural genomics, mcsg, unknown function
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 29186.70

構造登録者

Sanishvili, R.,Savchenko, A.,Skarina, T.,Edwards, A.,Joachimiak, A.,Yakunin, A.,Midwest Center for Structural Genomics (MCSG) (登録日: 2002-06-26, 公開日: 2003-01-21, 最終更新日: 2024-12-25)

主引用文献

Sanishvili, R.,Yakunin, A.F.,Laskowski, R.A.,Skarina, T.,Evdokimova, E.,Doherty-Kirby, A.,Lajoie, G.A.,Thornton, J.M.,Arrowsmith, C.H.,Savchenko, A.,Joachimiak, A.,Edwards, A.M.
Integrating structure, bioinformatics, and enzymology to discover function: BioH, a new carboxylesterase from Escherichia coli.
J.Biol.Chem., 278:26039-26045, 2003

PubMed Abstract: Structural proteomics projects are generating three-dimensional structures of novel, uncharacterized proteins at an increasing rate. However, structure alone is often insufficient to deduce the specific biochemical function of a protein. Here we determined the function for a protein using a strategy that integrates structural and bioinformatics data with parallel experimental screening for enzymatic activity. BioH is involved in biotin biosynthesis in Escherichia coli and had no previously known biochemical function. The crystal structure of BioH was determined at 1.7 A resolution. An automated procedure was used to compare the structure of BioH with structural templates from a variety of different enzyme active sites. This screen identified a catalytic triad (Ser82, His235, and Asp207) with a configuration similar to that of the catalytic triad of hydrolases. Analysis of BioH with a panel of hydrolase assays revealed a carboxylesterase activity with a preference for short acyl chain substrates. The combined use of structural bioinformatics with experimental screens for detecting enzyme activity could greatly enhance the rate at which function is determined from structure.

PubMed: 12732651
DOI: 10.1074/jbc.M303867200

実験手法

X-RAY DIFFRACTION (1.7 Å)