1yuo
From Proteopedia
(New page: 200px<br /> <applet load="1yuo" size="450" color="white" frame="true" align="right" spinBox="true" caption="1yuo, resolution 1.95Å" /> '''Optimisation of the...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1yuo.gif|left|200px]]<br /> | + | [[Image:1yuo.gif|left|200px]]<br /><applet load="1yuo" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1yuo" size=" | + | |
caption="1yuo, resolution 1.95Å" /> | caption="1yuo, resolution 1.95Å" /> | ||
'''Optimisation of the surface electrostatics as a strategy for cold adaptation of uracil-DNA N-glycosylase (UNG)from atlantic cod (Gadus morhua)'''<br /> | '''Optimisation of the surface electrostatics as a strategy for cold adaptation of uracil-DNA N-glycosylase (UNG)from atlantic cod (Gadus morhua)'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Cold-adapted enzymes are characterised by an increased catalytic | + | 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== | ==Disease== | ||
| Line 11: | Line 10: | ||
==About this Structure== | ==About this Structure== | ||
| - | 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:// | + | 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]. |
==Reference== | ==Reference== | ||
| Line 22: | Line 21: | ||
[[Category: Moe, E.]] | [[Category: Moe, E.]] | ||
[[Category: Olufsen, M.]] | [[Category: Olufsen, M.]] | ||
| - | [[Category: Riise, E | + | [[Category: Riise, E K.]] |
| - | [[Category: Smalas, A | + | [[Category: Smalas, A O.]] |
| - | [[Category: Willassen, N | + | [[Category: Willassen, N P.]] |
[[Category: cold adaptation]] | [[Category: cold adaptation]] | ||
[[Category: ung]] | [[Category: ung]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:09:17 2008'' |
Revision as of 14:09, 21 February 2008
|
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. Active as Uridine nucleosidase, with EC number 3.2.2.3 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
Page seeded by OCA on Thu Feb 21 16:09:17 2008
