Sandbox Reserved 342
From Proteopedia
| Line 6: | Line 6: | ||
| - | == ''' | + | == '''XANTHINE-GUANINE PHOSPHORIBOSYLTRANSFERASE''' == |
| Line 15: | Line 15: | ||
| - | = | + | =Structure= |
| + | PRTase structures fall into two groups, type I and Type II<ref name="Vos"/>. | ||
| + | XGTPase has a conserved sequence, 85-IVIDDLVDTG-94, which is called the PRib-PP (5-phospho-a-D-ribosyl-1-pyrophosphate) binding site<ref name="Vos"/>. This binding site features two adjacent acidic residues, which are surrounded by hydrophobic residues<ref name="Vos"/>. There s five-stranded b-sheet surrounded by three or four a-helices that creates a conserved structural core containing the PRib-PP binding site<ref name="Vos"/> | ||
| - | + | =Function= | |
| - | = | + | |
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"/>. | ||
| Line 25: | Line 26: | ||
<scene name='Sandbox_Reserved_342/Trial/1'>TextToBeDisplayed</scene>=MECHANISM= | <scene name='Sandbox_Reserved_342/Trial/1'>TextToBeDisplayed</scene>=MECHANISM= | ||
| - | == | + | ==Recognition== |
| - | == | + | ==Catalysis== |
Magnesium and other divalent cations are necessary for catalysis<ref name="Vos"/>. | Magnesium and other divalent cations are necessary for catalysis<ref name="Vos"/>. | ||
| - | = | + | =Importance= |
<Structure load='1a96' size='300' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' /> | <Structure load='1a96' size='300' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' /> | ||
| - | =''' | + | ='''Additional Resources'''= |
=References= | =References= | ||
<references/> | <references/> | ||
Revision as of 01:39, 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 |
| |||||||||
| 1a96, resolution 2.00Å () | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Ligands: | , , , | ||||||||
| Gene: | GPT (Escherichia coli) | ||||||||
| Activity: | Xanthine phosphoribosyltransferase, with EC number 2.4.2.22 | ||||||||
| |||||||||
| |||||||||
| 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 s five-stranded b-sheet surrounded by three or four a-helices that creates a conserved structural core containing the PRib-PP binding site[1]
Function
XGRT is an enzyme that catalyzes the conversion of guanine, xanthine, and sometimes hypoxanthine, to GMP, XMP, and IMP [1].
=MECHANISM=
Recognition
Catalysis
Magnesium and other divalent cations are necessary for catalysis[1].
Importance
|
