1okb
From Proteopedia
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| - | [[Image:1okb.jpg|left|200px]]<br /><applet load="1okb" size=" | + | [[Image:1okb.jpg|left|200px]]<br /><applet load="1okb" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1okb, resolution 1.90Å" /> | caption="1okb, resolution 1.90Å" /> | ||
'''CRYSTAL STRUCTURE OF URACIL-DNA GLYCOSYLASE FROM ATLANTIC COD (GADUS MORHUA)'''<br /> | '''CRYSTAL STRUCTURE OF URACIL-DNA GLYCOSYLASE FROM ATLANTIC COD (GADUS MORHUA)'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1OKB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Gadus_morhua Gadus morhua] with CL and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Uridine_nucleosidase Uridine nucleosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.2.3 3.2.2.3] Known structural/functional Site: <scene name='pdbsite=AC1:Cl Binding Site For Chain B'>AC1</scene>. Full crystallographic information is available from [http:// | + | 1OKB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Gadus_morhua Gadus morhua] with <scene name='pdbligand=CL:'>CL</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Uridine_nucleosidase Uridine nucleosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.2.3 3.2.2.3] Known structural/functional Site: <scene name='pdbsite=AC1:Cl+Binding+Site+For+Chain+B'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OKB OCA]. |
==Reference== | ==Reference== | ||
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[[Category: uracil-dna glycosylase]] | [[Category: uracil-dna glycosylase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 09:59:13 2008'' |
Revision as of 07:59, 3 February 2008
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CRYSTAL STRUCTURE OF URACIL-DNA GLYCOSYLASE FROM ATLANTIC COD (GADUS MORHUA)
Overview
Uracil-DNA glycosylase (UDG; EC 3.2.2.3) is a DNA-repair protein that, catalyses the hydrolysis of promutagenic uracil residues from single- or, double-stranded DNA, generating free uracil and abasic DNA. The crystal, structure of the catalytic domain of cod uracil-DNA glycosylase (cUDG) has, been determined to 1.9 A resolution, with final R factors of 18.61 and, 20.57% for the working and test sets of reflections, respectively. This is, the first crystal structure of a uracil-DNA glycosylase from a, cold-adapted species and a detailed comparison with the human enzyme is, performed in order to rationalize the cold-adapted behaviour of the cod, enzyme at the structural level. The catalytic domain of cUDG comprises 223, residues, with a sequence identity to the human UDG of 75%. The tertiary, structures of the two enzymes are also similar, with an overall, displacement in main-chain atomic positions of 0.63 A. The amino-acid, substitutions and the differences in intramolecular hydrogen bonds, hydrophobic interactions, ion-pair interactions and electrostatic, potentials are compared and discussed in order to gain insight into the, factors that cause the increased activity and reduced thermostability of, the cod enzyme. In particular, the reduced number of strong ion-pair, interactions in the C-terminal half of cUDG is believed to greatly affect, the flexibility and/or stability. Increased positive electrostatic surface, potential on the DNA-facing side of cUDG seems to be responsible for, increasing the affinity for the negatively charged DNA compared with that, of hUDG.
About this Structure
1OKB is a Single protein structure of sequence from Gadus morhua with and as ligands. Active as Uridine nucleosidase, with EC number 3.2.2.3 Known structural/functional Site: . Full crystallographic information is available from OCA.
Reference
The structure of uracil-DNA glycosylase from Atlantic cod (Gadus morhua) reveals cold-adaptation features., Leiros I, Moe E, Lanes O, Smalas AO, Willassen NP, Acta Crystallogr D Biol Crystallogr. 2003 Aug;59(Pt 8):1357-65. Epub 2003, Jul 23. PMID:12876336
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