On the structure of hisH: Protein structure prediction in the context of structural and functional genomics

P. O’donoghue, R. E. Amaro, Z. Luthey-Schulten

Research output: Contribution to journalArticle

Abstract

We predict a structure of the glutamine amido-transferase subunit (hisH) of imidazole glycerol phosphate synthase (IGPS) which catalyzes the fifth step of the histidine biosynthesis in Escherichia coli. The model is constructed using an energy-based threading program augmented by a multiple sequence to structure profile analysis. In developing our model we identified a conserved core region within hisH and a variable domain which is the likely site of interaction with the synthase subunit (hisF) of IGPS. Information available from structural and functional genomics studies was used to improve the structure prediction, to discuss parallels between histidine biosynthesis and other amino acid and nucleotide metabolic pathways, and to better understand the protein-protein interactions between the hisH and hisF domains of IGPS. This work allows us to develop a preliminary model for the structure of the entire IGPS holoenzyme.

Original languageEnglish (US)
Pages (from-to)257-268
Number of pages12
JournalJournal of Structural Biology
Volume134
Issue number2-3
DOIs
StatePublished - Jan 1 2001

Keywords

  • Glutamine amidotransferase
  • HisH
  • Imidazole glycerol phosphate synthase
  • Profile analysis
  • Protein structure prediction
  • Structural and functional genomics
  • Threading

ASJC Scopus subject areas

  • Structural Biology

Fingerprint Dive into the research topics of 'On the structure of hisH: Protein structure prediction in the context of structural and functional genomics'. Together they form a unique fingerprint.

  • Cite this