1A7J

PHOSPHORIBULOKINASE FROM RHODOBACTER SPHEROIDES

1A7J の概要

• エントリーDOI: 10.2210/pdb1a7j/pdb
• 分子名称: PHOSPHORIBULOKINASE, SULFATE ION (3 entities in total)
• 機能のキーワード: transferase, kinase, calvin cycle
• 由来する生物種: Rhodobacter sphaeroides
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 32806.03

構造登録者

Harrison, D.H.T.,Runquist, J.,Holub, A.,Miziorko, H. (登録日: 1998-03-16, 公開日: 1998-06-17, 最終更新日: 2024-02-07)

主引用文献

Harrison, D.H.,Runquist, J.A.,Holub, A.,Miziorko, H.M.
The crystal structure of phosphoribulokinase from Rhodobacter sphaeroides reveals a fold similar to that of adenylate kinase.
Biochemistry, 37:5074-5085, 1998

PubMed Abstract: The essential photosynthetic enzyme phosphoribulokinase (PRK) is responsible for the conversion of ribulose 5-phosphate (Ru5P) to ribulose 1,5-bisphosphate, the substrate for the CO2 fixing enzyme ribulose 1,5-bisphosphate carboxylase/oxygenase (Rubisco). We have determined the structure of the octameric bacterial form of PRK to a resolution of 2.5 A. The protein is folded into a seven-member mixed beta-sheet surrounded by alpha-helices, giving the overall appearance of the nucleotide monophosphate family of kinases. Homology with the nucleotide monophosphate kinases suggests a number of amino acid residues that are likely to be important in catalysis and suggests the roles of some amino acid residues that have been mutated prior to the determination of the structure. Further, sequence identity across eukaryotic and prokaryotic species and a calculation of the buried surface area suggests the identity within the octamer of a dimer conserved throughout evolution. The width of the groove leading to the active site is consistent with an oriented molecule of thioredoxin controlling the oxidation state of two cysteines that regulate activity in the eukaryotic enzymes. Although neither Asp 42 nor Asp 169 can be definitively assigned as the catalytic base, the crystal structure suggests the location of a ribulose 5-phosphate binding site and suggests a role for several of the conserved basic residues.

PubMed: 9548738
DOI: 10.1021/bi972805y

実験手法

X-RAY DIFFRACTION (2.5 Å)