Sandbox Reserved 342
This Sandbox is Reserved from January 10, 2010, through April 10, 2011 for use in BCMB 307-Proteins course taught by Andrea Gorrell at the University of Northern British Columbia, Prince George, BC, Canada. |
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1a96, resolution 2.00Å () | |||||||||
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Ligands: | , , , | ||||||||
Gene: | GPT (Escherichia coli) | ||||||||
Activity: | Xanthine phosphoribosyltransferase, with EC number 2.4.2.22 | ||||||||
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Resources: | FirstGlance, OCA, RCSB, PDBsum | ||||||||
Coordinates: | save as pdb, mmCIF, xml |
XANTHINE-GUANINE PHOSPHORIBOSYLTRANSFERASEXANTHINE-GUANINE PHOSPHORIBOSYLTRANSFERASE
IntroductionIntroduction
Xanthine-guanine Phosphoribosyltansferase (XGPRT) is one of three purine phosphoribosyltransferases (PRTases) that are part of the purine salvage pathway in Escherichia coli[1]; the other two PRTases in the pathway are HPRT and APRT[1]
StructureStructure
PRTase structures fall into two groups, type I and Type II[1]. XGTPase has a conserved sequence,, which is called the PRib-PP (5-phospho-a-D-ribosyl-1-pyrophosphate) binding site[1]. This binding site features two adjacent acidic residues, which are surrounded by hydrophobic residues[1]. There is a five-stranded b-sheet surrounded by three or four a-helices that creates a conserved structural core containing the PRib-PP binding site[1]. Another region of the sequence in XGTPase forms a lobe, which is involved in substrate recognition[1].
FunctionFunction
XGRT is an enzyme that catalyzes the conversion of guanine, xanthine, and sometimes hypoxanthine, to GMP, XMP, and IMP [1].
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MECHANISMMECHANISM
RecognitionRecognition
CatalysisCatalysis
Magnesium and other divalent cations are necessary for catalysis[1].