2QB6

Saccharomyces cerevisiae cytosolic exopolyphosphatase, sulfate complex

2QB6 の概要

• エントリーDOI: 10.2210/pdb2qb6/pdb
• 関連するPDBエントリー: 2QB7 2QB8
• 分子名称: Exopolyphosphatase, MANGANESE (II) ION, SULFATE ION, ... (7 entities in total)
• 機能のキーワード: a/b/a structure, dhh family phosphatase, hydrolase
• 由来する生物種: Saccharomyces cerevisiae (baker's yeast)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 90954.04

構造登録者

White, S.A.,Ugochukwu, E. (登録日: 2007-06-16, 公開日: 2007-12-11, 最終更新日: 2024-02-21)

主引用文献

Ugochukwu, E.,Lovering, A.L.,Mather, O.C.,Young, T.W.,White, S.A.
The crystal structure of the cytosolic exopolyphosphatase from Saccharomyces cerevisiae reveals the basis for substrate specificity.
J.Mol.Biol., 371:1007-1021, 2007

PubMed Abstract: Inorganic long-chain polyphosphate is a ubiquitous linear polymer in biology, consisting of many phosphate moieties linked by phosphoanhydride bonds. It is synthesized by polyphosphate kinase, and metabolised by a number of enzymes, including exo- and endopolyphosphatases. The Saccharomyces cerevisiae gene PPX1 encodes for a 45 kDa, metal-dependent, cytosolic exopolyphosphatase that processively cleaves the terminal phosphate group from the polyphosphate chain, until inorganic pyrophosphate is all that remains. PPX1 belongs to the DHH family of phosphoesterases, which includes: family-2 inorganic pyrophosphatases, found in Gram-positive bacteria; prune, a cyclic AMPase; and RecJ, a single-stranded DNA exonuclease. We describe the high-resolution X-ray structures of yeast PPX1, solved using the multiple isomorphous replacement with anomalous scattering (MIRAS) technique, and its complexes with phosphate (1.6 A), sulphate (1.8 A) and ATP (1.9 A). Yeast PPX1 folds into two domains, and the structures reveal a strong similarity to the family-2 inorganic pyrophosphatases, particularly in the active-site region. A large, extended channel formed at the interface of the N and C-terminal domains is lined with positively charged amino acids and represents a conduit for polyphosphate and the site of phosphate hydrolysis. Structural comparisons with the inorganic pyrophosphatases and analysis of the ligand-bound complexes lead us to propose a hydrolysis mechanism. Finally, we discuss a structural basis for substrate selectivity and processivity.

PubMed: 17599355
DOI: 10.1016/j.jmb.2007.05.066

実験手法

X-RAY DIFFRACTION (1.8 Å)