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PDBsum entry 1hgx
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Transferase (glycosyltransferase)
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PDB id
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1hgx
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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Crystal structure of the hypoxanthine-Guanine-Xanthine phosphoribosyltransferase from the protozoan parasite tritrichomonas foetus.
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Authors
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J.R.Somoza,
M.S.Chin,
P.J.Focia,
C.C.Wang,
R.J.Fletterick.
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Ref.
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Biochemistry, 1996,
35,
7032-7040.
[DOI no: ]
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PubMed id
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Note In the PDB file this reference is
annotated as "TO BE PUBLISHED".
The citation details given above were identified by an automated
search of PubMed on title and author
names, giving a
percentage match of
95%.
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Abstract
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The crystal structure of the hypoxanthine-guanine-xanthine
phosphoribosyltransferase (HGXPRTase) from Tritrichomonas foetus has been
determined and refined against X-ray data to 1.9 A resolution. T. foetus
HGXPRTase crystallizes as an asymmetric dimer, with GMP bound to only one of the
two molecules that form the asymmetric unit. Each molecule of HGXPRTase is
formed by two lobes joined by a short "hinge" region, and the GMP binds in a
cavity between the two lobes. A comparison of the two molecules in the
asymmetric unit shows that the hinge region is flexible and that ligand binding
affects the relative positions of the two lobes. The binding of GMP brings the
two lobes closer together, rotating one lobe by about 5 degrees relative to the
other. T. foetus appears to depend on HGXPRTase for its supply of GMP, making
this enzyme a target for antiparasite drug design. A comparison of the
structures of T. foetus HGXPRTase and human HGPRTase reveals that, while these
enzymes retain a similar polypeptide fold, there are substantial differences
between the active sites of these two homologs. These differences suggest that
it will be possible to find compounds that selectively inhibit the parasite
enzyme.
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Secondary reference #1
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Title
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Isolation, Sequencing and expression of the gene encoding hypoxanthine-Guanine-Xanthine phosphoribosyltransferase of tritrichomonas foetus.
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Authors
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M.S.Chin,
C.C.Wang.
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Ref.
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Mol Biochem Parasitol, 1994,
63,
221-229.
[DOI no: ]
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PubMed id
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