1hmp
From Proteopedia
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| - | [[Image:1hmp.gif|left|200px]] | + | [[Image:1hmp.gif|left|200px]] |
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| - | '''THE CRYSTAL STRUCTURE OF HUMAN HYPOXANTHINE-GUANINE PHOSPHORIBOSYLTRANSFERASE WITH BOUND GMP''' | + | {{Structure |
| + | |PDB= 1hmp |SIZE=350|CAPTION= <scene name='initialview01'>1hmp</scene>, resolution 2.5Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=5GP:GUANOSINE-5'-MONOPHOSPHATE'>5GP</scene> | ||
| + | |ACTIVITY= [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] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''THE CRYSTAL STRUCTURE OF HUMAN HYPOXANTHINE-GUANINE PHOSPHORIBOSYLTRANSFERASE WITH BOUND GMP''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1HMP is a [ | + | 1HMP is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HMP OCA]. |
==Reference== | ==Reference== | ||
| - | The crystal structure of human hypoxanthine-guanine phosphoribosyltransferase with bound GMP., Eads JC, Scapin G, Xu Y, Grubmeyer C, Sacchettini JC, Cell. 1994 Jul 29;78(2):325-34. PMID:[http:// | + | The crystal structure of human hypoxanthine-guanine phosphoribosyltransferase with bound GMP., Eads JC, Scapin G, Xu Y, Grubmeyer C, Sacchettini JC, Cell. 1994 Jul 29;78(2):325-34. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8044844 8044844] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Hypoxanthine phosphoribosyltransferase]] | [[Category: Hypoxanthine phosphoribosyltransferase]] | ||
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[[Category: transferase (glycosyltransferase)]] | [[Category: transferase (glycosyltransferase)]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:39:02 2008'' |
Revision as of 09:39, 20 March 2008
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| , resolution 2.5Å | |||||||
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| Ligands: | |||||||
| Activity: | Hypoxanthine phosphoribosyltransferase, with EC number 2.4.2.8 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
THE CRYSTAL STRUCTURE OF HUMAN HYPOXANTHINE-GUANINE PHOSPHORIBOSYLTRANSFERASE WITH BOUND GMP
Contents |
Overview
The crystal structure of HGPRTase with bound GMP has been determined and refined to 2.5 A resolution. The enzyme has a core alpha/beta structure resembling the nucleotide-binding fold of dehydrogenases, and a second lobe composed of residues from the amino and carboxy termini. The GMP molecule binds in an anti conformation in a solvent-exposed cleft of the enzyme. Lys-165, which forms a hydrogen bond to O6 of GMP, appears to be critical for determining the specificity for guanine and hypoxanthine over adenine. The location of active site residues also provides evidence for a possible mechanism for general base-assisted HGPRTase catalysis. A rationalization of the effects on stability and activity of naturally occurring single amino acid mutations of HGPRTase is presented, including a discussion of several mutations at the active site that lead to Lesch-Nyhan syndrome.
Disease
Known diseases associated with this structure: HPRT-related gout OMIM:[308000], Lesch-Nyhan syndrome, 300322, OMIM:[308000]
About this Structure
1HMP is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
The crystal structure of human hypoxanthine-guanine phosphoribosyltransferase with bound GMP., Eads JC, Scapin G, Xu Y, Grubmeyer C, Sacchettini JC, Cell. 1994 Jul 29;78(2):325-34. PMID:8044844
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