1AQF

PYRUVATE KINASE FROM RABBIT MUSCLE WITH MG, K, AND L-PHOSPHOLACTATE

1AQF の概要

• エントリーDOI: 10.2210/pdb1aqf/pdb
• 分子名称: PYRUVATE KINASE, POTASSIUM ION, MAGNESIUM ION, ... (5 entities in total)
• 機能のキーワード: transferase, pyruvate kinase, rabbit muscle, domain movement, potassium binding
• 由来する生物種: Oryctolagus cuniculus (rabbit)
• 細胞内の位置: Cytoplasm (By similarity): P11974
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 465858.25

構造登録者

Larsen, T.M.,Benning, M.M.,Wesenberg, G.E.,Rayment, I.,Reed, G.H. (登録日: 1997-07-29, 公開日: 1998-09-16, 最終更新日: 2024-02-07)

主引用文献

Larsen, T.M.,Benning, M.M.,Wesenberg, G.E.,Rayment, I.,Reed, G.H.
Ligand-induced domain movement in pyruvate kinase: structure of the enzyme from rabbit muscle with Mg2+, K+, and L-phospholactate at 2.7 A resolution.
Arch.Biochem.Biophys., 345:199-206, 1997

PubMed Abstract: The structure of rabbit muscle pyruvate kinase crystallized as a complex with Mg2+, K+, and L-phospholactate (L-P-lactate) has been solved and refined to 2.7 A resolution. The crystals, grown from solutions of polyethylene glycol 8000 at pH 7.5, belong to the space group P2(1) and have unit cell parameters a = 144.4 A, b = 112.6 A, c = 171.2 A, and beta = 93.7 degrees. The asymmetric unit contains two tetramers. The crystal structure reveals that the eight subunits within the asymmetric unit adopt several different conformations. These conformations are characterized by differences in the relative positions of protein domains A and B, resulting in different degrees of closure of the active site cleft that occupies the interface between these two domains. The global conformational differences may be described as rotations of the B domain with respect to the (beta/alpha)8-barrel of the A domain. Carbon atoms of the backbone in domain B rotate >20 degrees from the most open to the most closed subunit. The different conformations among subunits within the asymmetric unit are accompanied by 3-3.8 A shifts in the position of Mg2+ and a significant change in the orientation of the phenyl ring of Phe 243. In all of the subunits, Mg2+ coordinates to the protein through the carboxylate side chains of Glu 271 and Asp 295. In the subunit having the most closed conformation, Mg2+ also coordinates to the carboxylate oxygen, the bridging ester oxygen, and a nonbridging phosphoryl oxygen of L-P-lactate. Mg2+ to L-P-lactate coordination is missing in subunits exhibiting a more open conformation. K+ coordinates to four protein ligands and to a phosphoryl oxygen of the L-P-lactate. The position and liganding of K+ are unaffected by the different conformations of the subunits. The side chain of Arg 72, Mg2+, and K+ provides a locus of positive charge for the phosphate moiety of the analog in the closed subunit.

PubMed: 9308890
DOI: 10.1006/abbi.1997.0257

実験手法

X-RAY DIFFRACTION (2.7 Å)