1VZW

Crystal structure of the bifunctional protein Pria

1VZW の概要

• エントリーDOI: 10.2210/pdb1vzw/pdb
• 分子名称: PHOSPHORIBOSYL ISOMERASE A, SULFATE ION, GLYCEROL, ... (4 entities in total)
• 機能のキーワード: isomerase, histidine biosynthesis, tryptophan biosynthesis
• 由来する生物種: STREPTOMYCES COELICOLOR
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 25786.91

構造登録者

Kuper, J.,Wilmanns, M. (登録日: 2004-05-27, 公開日: 2005-01-19, 最終更新日: 2023-12-13)

主引用文献

Kuper, J.,Doenges, C.,Wilmanns, M.
Two-Fold Repeated (Beta-Alpha)(4) Half-Barrels May Provide a Molecular Tool for Dual Substrate Specificity
Embo Rep., 6:134-, 2005

PubMed Abstract: Some bacterial genomes contain an incomplete set of genes encoding phosphoribosyl isomerases, raising the question of whether there exists broadened substrate specificity for the missing gene products. To investigate the underlying molecular principles of this hypothesis, we have determined the crystal structure of the bifunctional enzyme PriA from Streptomyces coelicolor at 1.8 A resolution. It consists of a (betaalpha)(8)-barrel fold that is assembled by two symmetric (betaalpha)(4) half-barrels. The structure shows how its active site may catalyse the isomerization reactions of two different substrates, and we provide a plausible model of how the smaller of the two substrates could be bound in two different orientations. Our findings expand the half-barrel ancestor concept by demonstrating that symmetry-related half-barrels could provide a smart solution to cope with dual substrate specificity. The data may help to unravel molecular rationales regarding how organisms with miniature genomes can keep central biological pathways functional.

PubMed: 15654319
DOI: 10.1038/SJ.EMBOR.7400330

実験手法

X-RAY DIFFRACTION (1.8 Å)