Crystal structure of human riboflavin kinase reveals a β barrel fold and a novel active site arch

Subramanian Karthikeyan, Qingxian Zhou, Faika Mseeh, Nick V. Grishin, Andrei L. Osterman, Hong Zhang

Research output: Contribution to journalArticle

55 Scopus citations

Abstract

Riboflavin kinase (RFK) is an essential enzyme catalyzing the phosphorylation of riboflavin (vitamin B2) to form FMN, an obligatory step in vitamin B2 utilization and flavin cofactor synthesis. The structure of human RFK revealed a six-stranded antiparallel β barrel core structurally similar to the riboflavin synthase/ferredoxin reductase FAD binding domain fold. The binding site of an intrinsically bound MgADP defines a novel nucleotide binding motif that encompasses a loop, a 310 helix, and a reverse turn followed by a short β strand. This active site loop forms an arch with ATP and riboflavin binding at the opposite side and the phosphoryl transfer appears to occur through the hole underneath the arch. The invariant residues Asn36 and Glu86 are implicated in the catalysis.

Original languageEnglish (US)
Pages (from-to)265-273
Number of pages9
JournalStructure
Volume11
Issue number3
DOIs
StatePublished - Mar 1 2003

Keywords

  • Crystal structure
  • Flavocoenzyme biosynthesis
  • Nucleotide binding
  • Phosphoryl transfer
  • Riboflavin kinase
  • β barrel

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology

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