Document Detail

Multiple crystal forms of hexokinase I: new insights regarding conformational dynamics, subunit interactions, and membrane association.
MedLine Citation:
PMID:  9738448     Owner:  NLM     Status:  MEDLINE    
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.
A E Aleshin; H J Fromm; R B Honzatko
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Publication Detail:
Type:  Journal Article; Research Support, U.S. Gov't, Non-P.H.S.; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  FEBS letters     Volume:  434     ISSN:  0014-5793     ISO Abbreviation:  FEBS Lett.     Publication Date:  1998 Aug 
Date Detail:
Created Date:  1998-09-29     Completed Date:  1998-09-29     Revised Date:  2007-11-14    
Medline Journal Info:
Nlm Unique ID:  0155157     Medline TA:  FEBS Lett     Country:  NETHERLANDS    
Other Details:
Languages:  eng     Pagination:  42-6     Citation Subset:  IM    
Department of Biochemistry and Biophysics, Iowa State University, Ames 50011, USA.
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MeSH Terms
Cell Membrane / metabolism*
Crystallography, X-Ray
Hexokinase / chemistry*,  metabolism
Membrane Proteins / chemistry,  metabolism
Protein Conformation*
Recombinant Proteins / chemistry,  metabolism
Grant Support
Reg. No./Substance:
0/Membrane Proteins; 0/Recombinant Proteins; EC

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