1yuo

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[[Image:1yuo.gif|left|200px]]<br /><applet load="1yuo" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1yuo.gif|left|200px]]
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caption="1yuo, resolution 1.95&Aring;" />
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'''Optimisation of the surface electrostatics as a strategy for cold adaptation of uracil-DNA N-glycosylase (UNG)from atlantic cod (Gadus morhua)'''<br />
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{{Structure
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|PDB= 1yuo |SIZE=350|CAPTION= <scene name='initialview01'>1yuo</scene>, resolution 1.95&Aring;
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|SITE=
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|LIGAND=
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|ACTIVITY= [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]
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|GENE= UNG ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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}}
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'''Optimisation of the surface electrostatics as a strategy for cold adaptation of uracil-DNA N-glycosylase (UNG)from atlantic cod (Gadus morhua)'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1YUO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. 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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YUO OCA].
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1YUO 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=1YUO OCA].
==Reference==
==Reference==
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Optimisation of the surface electrostatics as a strategy for cold adaptation of uracil-DNA N-glycosylase (UNG) from Atlantic cod (Gadus morhua)., Moe E, Leiros I, Riise EK, Olufsen M, Lanes O, Smalas A, Willassen NP, J Mol Biol. 2004 Nov 5;343(5):1221-30. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15491608 15491608]
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Optimisation of the surface electrostatics as a strategy for cold adaptation of uracil-DNA N-glycosylase (UNG) from Atlantic cod (Gadus morhua)., Moe E, Leiros I, Riise EK, Olufsen M, Lanes O, Smalas A, Willassen NP, J Mol Biol. 2004 Nov 5;343(5):1221-30. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15491608 15491608]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: ung]]
[[Category: ung]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:09:17 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:27:43 2008''

Revision as of 13:27, 20 March 2008


PDB ID 1yuo

Drag the structure with the mouse to rotate
, resolution 1.95Å
Gene: UNG (Homo sapiens)
Activity: Uridine nucleosidase, with EC number 3.2.2.3
Coordinates: save as pdb, mmCIF, xml



Optimisation of the surface electrostatics as a strategy for cold adaptation of uracil-DNA N-glycosylase (UNG)from atlantic cod (Gadus morhua)


Contents

Overview

Cold-adapted enzymes are characterised by an increased catalytic efficiency and reduced temperature stability compared to their mesophilic counterparts. Lately, it has been suggested that an optimisation of the electrostatic surface potential is a strategy for cold adaptation for some enzymes. A visualisation of the electrostatic surface potential of cold-adapted uracil-DNA N-glycosylase (cUNG) from Atlantic cod indicates a more positively charged surface near the active site compared to human UNG (hUNG). In order to investigate the importance of the altered surface potential for the cold-adapted features of cod UNG, six mutants have been characterised and compared to cUNG and hUNG. The cUNG quadruple mutant (V171E, K185V, H250Q and H275Y) and four corresponding single mutants all comprise substitutions of residues present in the human enzyme. A human UNG mutant, E171V, comprises the equivalent residue found in cod UNG. In addition, crystal structures of the single mutants V171E and E171V have been determined. Results from the study show that a more negative electrostatic surface potential reduces the activity and increases the stability of cod UNG, and suggest an optimisation of the surface potential as a strategy for cold-adaptation of this enzyme. Val171 in cod UNG is especially important in this respect.

Disease

Known diseases associated with this structure: Immunodeficiency with hyper IgM, type 4 OMIM:[191525]

About this Structure

1YUO is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Optimisation of the surface electrostatics as a strategy for cold adaptation of uracil-DNA N-glycosylase (UNG) from Atlantic cod (Gadus morhua)., Moe E, Leiros I, Riise EK, Olufsen M, Lanes O, Smalas A, Willassen NP, J Mol Biol. 2004 Nov 5;343(5):1221-30. PMID:15491608

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