Structure of yeast hexokinase. III. Low resolution structure of a second crystal form showing a different quaternary structure, heterologous interaction of subunits and substrate binding

Wayne F. Anderson*, Robert J. Fletterick, Thomas A. Steitz

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

31 Scopus citations

Abstract

A 7 Å resolution electron density map of a second crystal form (called BII) of yeast hexokinase B has been obtained. This crystal form, unlike the first crystal form (BI), binds nucleotide and sugar substrates. While the overall tertiary structure of each subunit appears to be largely the same in both crystal forms, the quaternary structure of the dimer is completely different in the two crystals. The two subunits in the crystallographic asymmetric unit of form BII are related by a molecular screw axis; that is, the two subunits are related by a 160 ° rotation and a 13 Å translation of one subunit relative to the other along the symmetry axis resulting in non-equivalent environments for the two chemically identical subunits. A deep cleft divides each subunit into two domains or lobes of roughly equal size. The helical regions which are clearly visible as rods of electron density in this map constitute at least 40 to 50% of the polypeptide chain and 70 to 80% of one of the lobes. At this resolution the molecule does not appear to be homologous in detail to other kinases such as phosphoglycerate kinase and adenylate kinase. Sugar substrates and inhibitors bind deeply in the cleft which separates the two lobes and produce substantial alterations in the protein structure.

Original languageEnglish (US)
Pages (from-to)261-264,IN21-IN25,265-269
JournalJournal of Molecular Biology
Volume86
Issue number2
DOIs
StatePublished - Jun 25 1974

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology

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