Crystal structure of a type II dehydroquinate dehydratase-like protein from Bifidobacterium longum

Samuel H. Light, Sankar N. Krishna, Raymond C. Bergan, Arnon Lavie, Wayne F. Anderson

Research output: Contribution to journalArticle

Abstract

Dehydroquinate dehydratase (DHQD) catalyzes the third step in the biosynthetic shikimate pathway. Here we identify a Bifidobacterium longum protein with high sequence homology to type II DHQDs but no detectable DHQD activity under standard assay conditions. A crystal structure reveals that the B. longum protein adopts a DHQD-like tertiary structure but a distinct quaternary state. Apparently forming a dimer, the B. longum protein lacks the active site aspartic acid contributed from a neighboring protomer in the type II DHQD dodecamer. Relating to the absence of protein-protein interactions established in the type II DHQD dodecameric assembly, substantial conformational changes distinguish the would-be active site of the B. longum protein. As B. longum possess no other genes with homology to known DHQDs, these findings imply a unique DHQD activity within B. longum.

Original languageEnglish (US)
Pages (from-to)25-30
Number of pages6
JournalJournal of Structural and Functional Genomics
Volume14
Issue number1
DOIs
StatePublished - Mar 1 2013

Keywords

  • Post-translational activation
  • Quaternary structure
  • Shikimate pathway
  • Structural genomics
  • X-ray crystal structure

ASJC Scopus subject areas

  • Structural Biology
  • Biochemistry
  • Genetics

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