1dhr
From Proteopedia
(New page: 200px<br /><applet load="1dhr" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dhr, resolution 2.3Å" /> '''CRYSTAL STRUCTURE OF ...) |
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| - | [[Image:1dhr.gif|left|200px]]<br /><applet load="1dhr" size=" | + | [[Image:1dhr.gif|left|200px]]<br /><applet load="1dhr" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1dhr, resolution 2.3Å" /> | caption="1dhr, resolution 2.3Å" /> | ||
'''CRYSTAL STRUCTURE OF RAT LIVER DIHYDROPTERIDINE REDUCTASE'''<br /> | '''CRYSTAL STRUCTURE OF RAT LIVER DIHYDROPTERIDINE REDUCTASE'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The structure of a binary complex of dihydropteridine reductase [DHPR; | + | The structure of a binary complex of dihydropteridine reductase [DHPR; NAD(P)H:6,7-dihydropteridine oxidoreductase, EC 1.6.99.7] with its cofactor, NADH, has been solved and refined to a final R factor of 15.4% by using 2.3 A diffraction data. DHPR is an alpha/beta protein with a Rossmann-type dinucleotide fold for NADH binding. Insertion of an extra threonine residue in the human enzyme is associated with severe symptoms of a variant form of phenylketonuria and maps to a tightly linked sequence of secondary-structural elements near the dimer interface. Dimerization is mediated by a four-helix bundle motif (two helices from each protomer) having an unusual right-handed twist. DHPR is structurally and mechanistically distinct from dihydrofolate reductase, appearing to more closely resemble certain nicotinamide dinucleotide-requiring flavin-dependent enzymes, such as glutathione reductase. |
==About this Structure== | ==About this Structure== | ||
| - | 1DHR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with NAD as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/6,7-dihydropteridine_reductase 6,7-dihydropteridine reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.5.1.34 1.5.1.34] Full crystallographic information is available from [http:// | + | 1DHR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with <scene name='pdbligand=NAD:'>NAD</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/6,7-dihydropteridine_reductase 6,7-dihydropteridine reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.5.1.34 1.5.1.34] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DHR OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Matthews, D | + | [[Category: Matthews, D A.]] |
| - | [[Category: Skinner, M | + | [[Category: Skinner, M M.]] |
| - | [[Category: Varughese, K | + | [[Category: Varughese, K I.]] |
| - | [[Category: Whiteley, J | + | [[Category: Whiteley, J M.]] |
| - | [[Category: Xuong, N | + | [[Category: Xuong, N H.]] |
[[Category: NAD]] | [[Category: NAD]] | ||
[[Category: oxidoreductase(acting on nadh or nadph)]] | [[Category: oxidoreductase(acting on nadh or nadph)]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:16:40 2008'' |
Revision as of 10:16, 21 February 2008
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CRYSTAL STRUCTURE OF RAT LIVER DIHYDROPTERIDINE REDUCTASE
Overview
The structure of a binary complex of dihydropteridine reductase [DHPR; NAD(P)H:6,7-dihydropteridine oxidoreductase, EC 1.6.99.7] with its cofactor, NADH, has been solved and refined to a final R factor of 15.4% by using 2.3 A diffraction data. DHPR is an alpha/beta protein with a Rossmann-type dinucleotide fold for NADH binding. Insertion of an extra threonine residue in the human enzyme is associated with severe symptoms of a variant form of phenylketonuria and maps to a tightly linked sequence of secondary-structural elements near the dimer interface. Dimerization is mediated by a four-helix bundle motif (two helices from each protomer) having an unusual right-handed twist. DHPR is structurally and mechanistically distinct from dihydrofolate reductase, appearing to more closely resemble certain nicotinamide dinucleotide-requiring flavin-dependent enzymes, such as glutathione reductase.
About this Structure
1DHR is a Single protein structure of sequence from Rattus norvegicus with as ligand. Active as 6,7-dihydropteridine reductase, with EC number 1.5.1.34 Full crystallographic information is available from OCA.
Reference
Crystal structure of rat liver dihydropteridine reductase., Varughese KI, Skinner MM, Whiteley JM, Matthews DA, Xuong NH, Proc Natl Acad Sci U S A. 1992 Jul 1;89(13):6080-4. PMID:1631094
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