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Literature summary extracted from

  • Kuettner, E.B.; Kettner, K.; Keim, A.; Svergun, D.I.; Volke, D.; Singer, D.; Hoffmann, R.; Mueller, E.C.; Otto, A.; Kriegel, T.M.; Straeter, N.
    Crystal structure of hexokinase KlHxk1 of Kluyveromyces lactis: a molecular basis for understanding the control of yeast hexokinase functions via covalent modification and oligomerization (2010), J. Biol. Chem., 285, 41019-41033.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.7.1.1 in five crystal forms, a symmetrical ring-shaped homodimer is observed, corresponding to the physiological dimer existing in solution as shown by small-angle X-ray scattering. The dimer has a head-to-tail arrangement such that the small domain of one subunit interacts with the large domain of the other subunit. Dimer formation requires favorable interactions of the 15 N-terminal amino acids that are part of the large domain with amino acids of the small domain of the opposite subunit, respectively Kluyveromyces lactis

Organism

EC Number Organism UniProt Comment Textmining
2.7.1.1 Kluyveromyces lactis P33284
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
2.7.1.1 phosphoprotein
-
 Kluyveromyces lactis

Purification (Commentary)

EC Number Purification (Comment) Organism
2.7.1.1 gel filtration Kluyveromyces lactis

Subunits

EC Number Subunits Comment Organism
2.7.1.1 homodimer crystal structure: The dimer has a head-to-tail arrangement such that the small domain of one subunit interacts with the large domain of the other subunit. Dimer formation requires favorable interactions of the 15 N-terminal amino acids that are part of the large domain with amino acids of the small domain of the opposite subunit, respectively Kluyveromyces lactis

Synonyms

EC Number Synonyms Comment Organism
2.7.1.1 KlHxk1
-
 Kluyveromyces lactis