3B8A

Crystal structure of yeast hexokinase PI in complex with glucose

3B8A の概要

• エントリーDOI: 10.2210/pdb3b8a/pdb
• 分子名称: Hexokinase-1, beta-D-glucopyranose, SULFATE ION, ... (4 entities in total)
• 機能のキーワード: induced fit, allosteric enzyme, atp-binding, glycolysis, kinase, nucleotide-binding, phosphorylation, 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: 54080.47

構造登録者

Kuser, P.,Cupri, F.,Bleicher, L.,Polikarpov, I. (登録日: 2007-10-31, 公開日: 2008-02-26, 最終更新日: 2023-08-30)

主引用文献

Kuser, P.,Cupri, F.,Bleicher, L.,Polikarpov, I.
Crystal structure of yeast hexokinase PI in complex with glucose: A classical "induced fit" example revised.
Proteins, 72:731-740, 2008

PubMed Abstract: Hexokinase is the first enzyme in the glycolytic pathway that catalyzes 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. Here we redetermined the crystal structure of yeast hexokinase PI from Saccharomyces cerevisiae as a complex with its substrate, glucose, and refined it at 2.95 A resolution. Comparison of the holo-PI yeast hexokinase and apo-hexokinase structures shows in detail the rigid body domain closure and specific loop movements as glucose binds and sheds more light on structural basis of the "induced fit" mechanism of reaction in the HK enzymatic action. We also performed statistical coupling analysis of the hexokinase family, which reveals two co-evolved continuous clusters of amino acid residues and shows that the evolutionary coupled amino acid residues are mostly confined to the active site and the hinge region, further supporting the importance of these parts of the protein for the enzymatic catalysis.

PubMed: 18260108
DOI: 10.1002/prot.21956

実験手法

X-RAY DIFFRACTION (2.95 Å)