1h5y
HISF PROTEIN FROM PYROBACULUM AEROPHILUM
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OverviewOverview
HisF (imidazole glycerol phosphate synthase) is an important branch-point, enzyme in the histidine biosynthetic pathway of microorganisms. Because of, its potential relevance for structure-based drug design, the crystal, structure of HisF from the hyperthermophilic archaeon Pyrobaculum, aerophilum has been determined. The structure was determined by molecular, replacement and refined at 2.0 A resolution to a crystallographic R factor, of 20.6% and a free R of 22.7%. The structure adopts a classic, (beta/alpha)(8) barrel fold and has networks of surface salt bridges that, may contribute to thermostability. The active site is marked out by the, presence of two bound phosphate ions and two glycerol molecules that, delineate a long groove at one end of the (beta/alpha)(8) barrel. The two, ... [(full description)]
About this StructureAbout this Structure
1H5Y is a [Single protein] structure of sequence from [Pyrobaculum aerophilum] with PO4 and GOL as [ligands]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
ReferenceReference
Structure of HisF, a histidine biosynthetic protein from Pyrobaculum aerophilum., Banfield MJ, Lott JS, Arcus VL, McCarthy AA, Baker EN, Acta Crystallogr D Biol Crystallogr. 2001 Nov;57(Pt 11):1518-25. Epub 2001, Oct 25. PMID:11679715
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