1ev7

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="1ev7" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ev7, resolution 2.38&Aring;" /> '''CRYSTAL STRUCTURE OF...)
Line 1: Line 1:
-
[[Image:1ev7.gif|left|200px]]<br /><applet load="1ev7" size="450" color="white" frame="true" align="right" spinBox="true"
+
[[Image:1ev7.gif|left|200px]]<br /><applet load="1ev7" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1ev7, resolution 2.38&Aring;" />
caption="1ev7, resolution 2.38&Aring;" />
'''CRYSTAL STRUCTURE OF DNA RESTRICTION ENDONUCLEASE NAEI'''<br />
'''CRYSTAL STRUCTURE OF DNA RESTRICTION ENDONUCLEASE NAEI'''<br />
==Overview==
==Overview==
-
NAE:I is transformed from DNA endonuclease to DNA topoisomerase and, recombinase by a single amino acid substitution. The crystal structure of, NAE:I was solved at 2.3 A resolution and shows that NAE:I is a dimeric, molecule with two domains per monomer. Each domain contains one potential, DNA recognition motif corresponding to either endonuclease or, topoisomerase activity. The N-terminal domain core folds like the other, type II restriction endonucleases as well as lambda-exonuclease and the, DNA repair enzymes MutH and Vsr, implying a common evolutionary origin and, catalytic mechanism. The C-terminal domain contains a catabolite activator, protein (CAP) motif present in many DNA-binding proteins, including the, type IA and type II topoisomerases. Thus, the NAE:I structure implies that, DNA processing enzymes evolved from a few common ancestors. NAE:I may be, an evolutionary bridge between endonuclease and DNA processing enzymes.
+
NAE:I is transformed from DNA endonuclease to DNA topoisomerase and recombinase by a single amino acid substitution. The crystal structure of NAE:I was solved at 2.3 A resolution and shows that NAE:I is a dimeric molecule with two domains per monomer. Each domain contains one potential DNA recognition motif corresponding to either endonuclease or topoisomerase activity. The N-terminal domain core folds like the other type II restriction endonucleases as well as lambda-exonuclease and the DNA repair enzymes MutH and Vsr, implying a common evolutionary origin and catalytic mechanism. The C-terminal domain contains a catabolite activator protein (CAP) motif present in many DNA-binding proteins, including the type IA and type II topoisomerases. Thus, the NAE:I structure implies that DNA processing enzymes evolved from a few common ancestors. NAE:I may be an evolutionary bridge between endonuclease and DNA processing enzymes.
==About this Structure==
==About this Structure==
-
1EV7 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Lechevalieria_aerocolonigenes Lechevalieria aerocolonigenes]. Active as [http://en.wikipedia.org/wiki/Type_II_site-specific_deoxyribonuclease Type II site-specific deoxyribonuclease], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.21.4 3.1.21.4] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1EV7 OCA].
+
1EV7 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Lechevalieria_aerocolonigenes Lechevalieria aerocolonigenes]. Active as [http://en.wikipedia.org/wiki/Type_II_site-specific_deoxyribonuclease Type II site-specific deoxyribonuclease], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.21.4 3.1.21.4] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EV7 OCA].
==Reference==
==Reference==
Line 15: Line 15:
[[Category: Type II site-specific deoxyribonuclease]]
[[Category: Type II site-specific deoxyribonuclease]]
[[Category: Chen, Y.]]
[[Category: Chen, Y.]]
-
[[Category: Colandene, J.D.]]
+
[[Category: Colandene, J D.]]
[[Category: Huai, Q.]]
[[Category: Huai, Q.]]
[[Category: Luo, F.]]
[[Category: Luo, F.]]
Line 25: Line 25:
[[Category: topoisomerase]]
[[Category: topoisomerase]]
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 14:20:42 2007''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:31:49 2008''

Revision as of 10:31, 21 February 2008


1ev7, resolution 2.38Å

Drag the structure with the mouse to rotate

CRYSTAL STRUCTURE OF DNA RESTRICTION ENDONUCLEASE NAEI

Overview

NAE:I is transformed from DNA endonuclease to DNA topoisomerase and recombinase by a single amino acid substitution. The crystal structure of NAE:I was solved at 2.3 A resolution and shows that NAE:I is a dimeric molecule with two domains per monomer. Each domain contains one potential DNA recognition motif corresponding to either endonuclease or topoisomerase activity. The N-terminal domain core folds like the other type II restriction endonucleases as well as lambda-exonuclease and the DNA repair enzymes MutH and Vsr, implying a common evolutionary origin and catalytic mechanism. The C-terminal domain contains a catabolite activator protein (CAP) motif present in many DNA-binding proteins, including the type IA and type II topoisomerases. Thus, the NAE:I structure implies that DNA processing enzymes evolved from a few common ancestors. NAE:I may be an evolutionary bridge between endonuclease and DNA processing enzymes.

About this Structure

1EV7 is a Single protein structure of sequence from Lechevalieria aerocolonigenes. Active as Type II site-specific deoxyribonuclease, with EC number 3.1.21.4 Full crystallographic information is available from OCA.

Reference

Crystal structure of NaeI-an evolutionary bridge between DNA endonuclease and topoisomerase., Huai Q, Colandene JD, Chen Y, Luo F, Zhao Y, Topal MD, Ke H, EMBO J. 2000 Jun 15;19(12):3110-8. PMID:10856254

Page seeded by OCA on Thu Feb 21 12:31:49 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools