1IG8

Crystal Structure of Yeast Hexokinase PII with the correct amino acid sequence

1IG8 の概要

• エントリーDOI: 10.2210/pdb1ig8/pdb
• 関連するPDBエントリー: 2yhx
• 分子名称: hexokinase PII, SULFATE ION (3 entities in total)
• 機能のキーワード: mixed alpha beta, two domains, cleft, transferase
• 由来する生物種: Saccharomyces cerevisiae (baker's yeast)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 54097.31

構造登録者

Kuser, P.R.,Krauchenco, S.,Antunes, O.A.,Polikarpov, I. (登録日: 2001-04-17, 公開日: 2001-05-02, 最終更新日: 2024-04-03)

主引用文献

Kuser, P.R.,Krauchenco, S.,Antunes, O.A.,Polikarpov, I.
The high resolution crystal structure of yeast hexokinase PII with the correct primary sequence provides new insights into its mechanism of action.
J.Biol.Chem., 275:20814-20821, 2000

PubMed Abstract: Hexokinase is the first enzyme in the glycolytic pathway, catalyzing the transfer of a phosphoryl group from ATP to glucose to form glucose 6-phosphate and ADP. Two yeast hexokinase isozymes are known, namely PI and PII. The crystal structure of yeast hexokinase PII from Saccharomyces cerevisiae without substrate or competitive inhibitor is determined and refined in a tetragonal crystal form at 2.2-A resolution. The folding of the peptide chain is very similar to that of Schistosoma mansoni and previous yeast hexokinase models despite only 30% sequence identity between them. Distinct differences in conformation are found that account for the absence of glucose in the binding site. Comparison of the current model with S. mansoni and yeast hexokinase PI structures both complexed with glucose shows in atomic detail the rigid body domain closure and specific loop movements as glucose binds. A hydrophobic channel formed by strictly conserved hydrophobic residues in the small domain of the hexokinase is identified. The channel's mouth is close to the active site and passes through the small domain to its surface. The possible role of the observed channel in proton transfer is discussed.

PubMed: 10749890
DOI: 10.1074/jbc.M910412199

実験手法

X-RAY DIFFRACTION (2.2 Å)