1h5y
|
HISF PROTEIN FROM PYROBACULUM AEROPHILUM
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, phosphate ions, 17 A apart, are bound to sequence-conserved structural, motifs that seem likely to provide much of the specificity for the two, phosphate groups of the HisF substrate. The two glycerol molecules bind in, the vicinity of other sequence-conserved residues that are likely to be, involved in binding and/or catalysis. Comparisons with the homologous HisF, from Thermatoga maritima reveal a displaced loop that may serve as a lid, over the active site.
About this StructureAbout this Structure
1H5Y is a Single protein structure of sequence from Pyrobaculum aerophilum with PO4 and GOL as ligands. Known structural/functional Site: . 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
Page seeded by OCA on Tue Dec 18 16:02:59 2007