A new crystal form of mouse thiamin pyrophosphokinase

Jing Yuan Liu, Thomas D. Hurley

Research output: Contribution to journalArticle

2 Scopus citations


Thiamin pyrophosphokinase (TPK) transfers a pyrophosphate group from ATP to the hydroxyl group of thiamin and produces thiamin pyrophosphate (TPP). TPP is the cofactor of metabolically important enzymes such as pyruvate dehydrogenase, α-ketoglutarate dehydrogenase, branched-chain α-keto acid dehydrogenase, transketolase and 2-hydroxyphytanoyl-CoA lyase. Thiamin deficiency results in Wernike-Korsakof Syndrome (WKS) due to neurological disorder and wet beriberi, a potentially fatal cardiovascular disease. Mouse TPK associates as a dimer revealed by previous solved crystallographic structures. In this study, we report mouse TPK complexed with TPP-Mg2+ and thiamin -Mg2+, respectively, in a new crystal form. In these two structures, four mouse TPK molecules were found in each asymmetric unit. Although we cannot rule out this tetramer form can be an artifact from crystal packing, mouse TPK tetramer has a more closed ATP binding pocket and has the potential to provide specific interactions between mouse TPK and ATP compared with the previous dimeric structure and is likely to be an active form.

Original languageEnglish (US)
Pages (from-to)111-118
Number of pages8
JournalInternational Journal of Biochemistry and Molecular Biology
Issue number2
StatePublished - Jun 10 2011


  • Crystal structure
  • Dimer
  • Protein oligomerization
  • Tetramer
  • Thiamin pyrophosphokinase (TPK)
  • Thiamin-Mg
  • TPP-Mg

ASJC Scopus subject areas

  • Molecular Biology
  • Biochemistry

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