On the structure of hisH: protein structure prediction in the context of structural and functional genomics.
We predict a structure of the glutamine amidotransferase 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.
O'Donoghue
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School of Chemical Sciences, University of Illinois, Urbana, Illinois 61801, USA.
Amaro
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Luthey-Schulten
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D000123:Acetyltransferases / Q000737:chemistry / Q000235:genetics; D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics*; D019295:Computational Biology; D004926:Escherichia coli / Q000201:enzymology / Q000235:genetics / Q000378:metabolism; D006639:Histidine / Q000096:biosynthesis; D006801:Humans; D008969:Molecular Sequence Data; D017434:Protein Structure, Tertiary / Q000235:genetics; D000637:Transaminases / Q000737:chemistry* / Q000235:genetics*
D001426:Bacterial Proteins; D006639:Histidine; D000123:Acetyltransferases; C020646:glutamate acetyltransferase; D000637:Transaminases; C053430:histidinol-phosphate aminotransferase