Multiple crystal forms of hexokinase I: new insights regarding conformational dynamics, subunit interactions, and membrane association

FEBS Letters

Honzatko, Richard B¹  Fromm, Herbert J¹  Aleshin, Alexander E¹ 

[1] Department of Biochemistry and Biophysics, 1210 Molecular Biology Bldg., Iowa State University, Ames, IA 50011, USA

关键词: Mammalian hexokinase;    Glycolysis;    Conformational dynamics;    Subunit interface;    Protein-membrane interaction;    Human;    Gluc-6-P;    glucose-6-phosphate;    Pi;    phosphate;   

DOI  :  10.1016/S0014-5793(98)00952-1

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Hexokinase I is comprised of homologous N- and C-terminal domains, and binds to the outer membrane of mitochondria. Reported here is the structure of a new crystal form of recombinant human hexokinase I, which complements existing crystal structures. Evidently, in some packing environments and even in the presence of glucose and glucose 6-phosphate the N-terminal domain (but not the C-terminal domain) can undergo oscillations between closed and partially opened conformations. Subunit interfaces, present in all known crystal forms of hexokinase I, promote the formation of linear chains of hexokinase I dimers. Presented is a model for membrane-associated hexokinase I, in which linear chains of hexokinase I dimers are stabilized by interactions with mitochondrial porin.

【 授权许可】

Unknown