1DKR

CRYSTAL STRUCTURES OF BACILLUS SUBTILIS PHOSPHORIBOSYLPYROPHOSPHATE SYNTHETASE: MOLECULAR BASIS OF ALLOSTERIC INHIBITION AND ACTIVATION.

1DKR の概要

• エントリーDOI: 10.2210/pdb1dkr/pdb
• 関連するPDBエントリー: 1DKU
• 分子名称: PHOSPHORIBOSYL PYROPHOSPHATE SYNTHETASE, SULFATE ION (3 entities in total)
• 機能のキーワード: domain duplication, open alpha beta domain structure, phosphoribosyltransferase type i fold., transferase
• 由来する生物種: Bacillus subtilis
• 細胞内の位置: Cytoplasm : P14193
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 70204.70

構造登録者

Eriksen, T.A.,Kadziola, A.,Bentsen, A.-K.,Harlow, K.W.,Larsen, S. (登録日: 1999-12-08, 公開日: 2000-04-05, 最終更新日: 2024-02-07)

主引用文献

Eriksen, T.A.,Kadziola, A.,Bentsen, A.K.,Harlow, K.W.,Larsen, S.
Structural basis for the function of Bacillus subtilis phosphoribosyl-pyrophosphate synthetase.
Nat.Struct.Biol., 7:303-308, 2000

PubMed Abstract: Here we report the first three-dimensional structure of a phosphoribosylpyrophosphate (PRPP) synthetase. PRPP is an essential intermediate in several biosynthetic pathways. Structures of the Bacillus subtilis PRPP synthetase in complex with analogs of the activator phosphate and the allosteric inhibitor ADP show that the functional form of the enzyme is a hexamer. The individual subunits fold into two domains, both of which resemble the type I phosphoribosyltransfereases. The active site is located between the two domains and includes residues from two subunits. Phosphate and ADP bind to the same regulatory site consisting of residues from three subunits of the hexamer. In addition to identifying residues important for binding substrates and effectors, the structures suggest a novel mode of allosteric regulation.

PubMed: 10742175
DOI: 10.1038/74069

実験手法

X-RAY DIFFRACTION (2.3 Å)