1vas

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /> <applet load="1vas" size="450" color="white" frame="true" align="right" spinBox="true" caption="1vas, resolution 2.750&Aring;" /> '''ATOMIC MODEL OF A ...)
Line 1: Line 1:
-
[[Image:1vas.gif|left|200px]]<br />
+
[[Image:1vas.gif|left|200px]]<br /><applet load="1vas" size="350" color="white" frame="true" align="right" spinBox="true"
-
<applet load="1vas" size="450" color="white" frame="true" align="right" spinBox="true"
+
caption="1vas, resolution 2.750&Aring;" />
caption="1vas, resolution 2.750&Aring;" />
'''ATOMIC MODEL OF A PYRIMIDINE DIMER SPECIFIC EXCISION REPAIR ENZYME COMPLEXED WITH A DNA SUBSTRATE: STRUCTURAL BASIS FOR DAMAGED DNA RECOGNITION'''<br />
'''ATOMIC MODEL OF A PYRIMIDINE DIMER SPECIFIC EXCISION REPAIR ENZYME COMPLEXED WITH A DNA SUBSTRATE: STRUCTURAL BASIS FOR DAMAGED DNA RECOGNITION'''<br />
==Overview==
==Overview==
-
T4 endonuclease V is a DNA repair enzyme from bacteriophage T4 that, catalyzes the first reaction step of the pyrimidine dimer-specific base, excision repair pathway. The crystal structure of this enzyme complexed, with a duplex DNA substrate, containing a thymine dimer, has been, determined at 2.75 A resolution. The atomic structure of the complex, reveals the unique conformation of the DNA duplex, which exhibits a sharp, kink with a 60 degree inclination at the central thymine dimer. The, adenine base complementary to the 5' side of the thymine dimer is, completely flipped out of the DNA duplex and trapped in a cavity on the, protein surface. These structural features allow an understanding of the, catalytic mechanism and implicate a general mechanism of how other repair, enzymes recognize damaged DNA duplexes.
+
T4 endonuclease V is a DNA repair enzyme from bacteriophage T4 that catalyzes the first reaction step of the pyrimidine dimer-specific base excision repair pathway. The crystal structure of this enzyme complexed with a duplex DNA substrate, containing a thymine dimer, has been determined at 2.75 A resolution. The atomic structure of the complex reveals the unique conformation of the DNA duplex, which exhibits a sharp kink with a 60 degree inclination at the central thymine dimer. The adenine base complementary to the 5' side of the thymine dimer is completely flipped out of the DNA duplex and trapped in a cavity on the protein surface. These structural features allow an understanding of the catalytic mechanism and implicate a general mechanism of how other repair enzymes recognize damaged DNA duplexes.
==About this Structure==
==About this Structure==
-
1VAS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacteriophage_t4 Bacteriophage t4]. The following page contains interesting information on the relation of 1VAS with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb91_1.html Thymine Dimers]]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1VAS OCA].
+
1VAS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacteriophage_t4 Bacteriophage t4]. The following page contains interesting information on the relation of 1VAS with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb91_1.html Thymine Dimers]]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VAS OCA].
==Reference==
==Reference==
Line 21: Line 20:
[[Category: Morikawa, K.]]
[[Category: Morikawa, K.]]
[[Category: Ohtsuka, E.]]
[[Category: Ohtsuka, E.]]
-
[[Category: Vassylyev, D.G.]]
+
[[Category: Vassylyev, D G.]]
[[Category: double helix]]
[[Category: double helix]]
[[Category: protein-dna complex]]
[[Category: protein-dna complex]]
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 18 09:06:52 2007''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:33:16 2008''

Revision as of 13:33, 21 February 2008


1vas, resolution 2.750Å

Drag the structure with the mouse to rotate

ATOMIC MODEL OF A PYRIMIDINE DIMER SPECIFIC EXCISION REPAIR ENZYME COMPLEXED WITH A DNA SUBSTRATE: STRUCTURAL BASIS FOR DAMAGED DNA RECOGNITION

Overview

T4 endonuclease V is a DNA repair enzyme from bacteriophage T4 that catalyzes the first reaction step of the pyrimidine dimer-specific base excision repair pathway. The crystal structure of this enzyme complexed with a duplex DNA substrate, containing a thymine dimer, has been determined at 2.75 A resolution. The atomic structure of the complex reveals the unique conformation of the DNA duplex, which exhibits a sharp kink with a 60 degree inclination at the central thymine dimer. The adenine base complementary to the 5' side of the thymine dimer is completely flipped out of the DNA duplex and trapped in a cavity on the protein surface. These structural features allow an understanding of the catalytic mechanism and implicate a general mechanism of how other repair enzymes recognize damaged DNA duplexes.

About this Structure

1VAS is a Single protein structure of sequence from Bacteriophage t4. The following page contains interesting information on the relation of 1VAS with [Thymine Dimers]. Full crystallographic information is available from OCA.

Reference

Atomic model of a pyrimidine dimer excision repair enzyme complexed with a DNA substrate: structural basis for damaged DNA recognition., Vassylyev DG, Kashiwagi T, Mikami Y, Ariyoshi M, Iwai S, Ohtsuka E, Morikawa K, Cell. 1995 Dec 1;83(5):773-82. PMID:8521494

Page seeded by OCA on Thu Feb 21 15:33:16 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools