EDD, a novel phosphotransferase domain common to mannose transporter EIIA, dihydroxyacetone kinase, and DegV

Lisa N. Kinch, Sara Cheek, Nick V. Grishin

Research output: Contribution to journalArticlepeer-review

12 Scopus citations

Abstract

Using a recently developed program (SCOPmap) designed to automatically assign new protein structures to existing evolutionary-based classification schemes, we identify a evolutionarily conserved domain (EDD) common to three different folds: mannose transporter EIIA domain (EIIA-man), dihydroxyacetone kinase (Dak), and DegV. Several lines of evidence support unification of these three folds into a single superfamily: statistically significant sequence similarity detected by PSI-BLAST; "closed structural grouping" using DALI Z-scores (each protein inside a group finds all other group members with scores higher than those to proteins outside the group) that includes only these proteins sharing a unique α-helical hairpin at the C-terminus and excludes all other proteins with similar topology; similar domain fusions connect Dak and DegV, and genomic neighborhood organizations connect Dak and EIIA-man. Finally, both Dak and EIIA-man perform similar phosphotransfer reactions, suggesting a phosphotransferase activity for the DegV-like family of proteins, whose function other than lipid binding revealed in the crystal structure remains unknown.

Original languageEnglish (US)
Pages (from-to)360-367
Number of pages8
JournalProtein Science
Volume14
Issue number2
DOIs
StatePublished - Feb 2005

Keywords

  • Dak1
  • Dak2
  • DegV
  • Dihydroxyacetone kinase
  • EDD domain
  • Homology detection
  • Mannose transporter EIIA
  • Protein classification
  • SCOPmap
  • Structure similarity

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology

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