Sandbox Reserved 342
From Proteopedia
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XGRT is an enzyme that catalyzes the conversion of guanine, xanthine, and sometimes hypoxanthine, to GMP, XMP, and IMP <ref name="Vos"/>. | XGRT is an enzyme that catalyzes the conversion of guanine, xanthine, and sometimes hypoxanthine, to GMP, XMP, and IMP <ref name="Vos"/>. | ||
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Revision as of 02:16, 3 April 2011
| 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. |
To get started:
More help: Help:Editing |
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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 PHOSPHORIBOSYLTRANSFERASE
Contents |
Introduction
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].
Structure
PRTase structures fall into two groups, type I and Type II[1]. XGTPase has a conserved sequence,85-IVIDDLVDTG-94, 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].
Function
XGRT is an enzyme that catalyzes the conversion of guanine, xanthine, and sometimes hypoxanthine, to GMP, XMP, and IMP [1].
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