1hgx
From Proteopedia
(New page: 200px<br /><applet load="1hgx" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hgx, resolution 1.9Å" /> '''HYPOXANTHINE-GUANINE-...) |
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| - | [[Image:1hgx.gif|left|200px]]<br /><applet load="1hgx" size=" | + | [[Image:1hgx.gif|left|200px]]<br /><applet load="1hgx" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1hgx, resolution 1.9Å" /> | caption="1hgx, resolution 1.9Å" /> | ||
'''HYPOXANTHINE-GUANINE-XANTHINE PHOSPHORIBOSYLTRANSFERASE (HGXPRTASE)'''<br /> | '''HYPOXANTHINE-GUANINE-XANTHINE PHOSPHORIBOSYLTRANSFERASE (HGXPRTASE)'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The crystal structure of the hypoxanthine-guanine-xanthine | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 1HGX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Tritrichomonas_foetus Tritrichomonas foetus] with SO4 and 5GP as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Hypoxanthine_phosphoribosyltransferase Hypoxanthine phosphoribosyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.2.8 2.4.2.8] Full crystallographic information is available from [http:// | + | 1HGX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Tritrichomonas_foetus Tritrichomonas foetus] with <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=5GP:'>5GP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Hypoxanthine_phosphoribosyltransferase Hypoxanthine phosphoribosyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.2.8 2.4.2.8] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HGX OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Tritrichomonas foetus]] | [[Category: Tritrichomonas foetus]] | ||
| - | [[Category: Fletterick, R | + | [[Category: Fletterick, R J.]] |
| - | [[Category: Somoza, J | + | [[Category: Somoza, J R.]] |
| - | [[Category: Wang, C | + | [[Category: Wang, C C.]] |
[[Category: 5GP]] | [[Category: 5GP]] | ||
[[Category: SO4]] | [[Category: SO4]] | ||
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[[Category: transferase]] | [[Category: transferase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:01:07 2008'' |
Revision as of 11:01, 21 February 2008
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HYPOXANTHINE-GUANINE-XANTHINE PHOSPHORIBOSYLTRANSFERASE (HGXPRTASE)
Overview
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.
About this Structure
1HGX is a Single protein structure of sequence from Tritrichomonas foetus with and as ligands. Active as Hypoxanthine phosphoribosyltransferase, with EC number 2.4.2.8 Full crystallographic information is available from OCA.
Reference
Crystal structure of the hypoxanthine-guanine-xanthine phosphoribosyltransferase from the protozoan parasite Tritrichomonas foetus., Somoza JR, Chin MS, Focia PJ, Wang CC, Fletterick RJ, Biochemistry. 1996 Jun 4;35(22):7032-40. PMID:8679528
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