This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.


Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1oyi

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1oyi.jpg|left|200px]]<br /><applet load="1oyi" size="350" color="white" frame="true" align="right" spinBox="true"
+
[[Image:1oyi.jpg|left|200px]]
-
caption="1oyi" />
+
 
-
'''Solution structure of the Z-DNA binding domain of the vaccinia virus gene E3L'''<br />
+
{{Structure
 +
|PDB= 1oyi |SIZE=350|CAPTION= <scene name='initialview01'>1oyi</scene>
 +
|SITE=
 +
|LIGAND=
 +
|ACTIVITY=
 +
|GENE= E3L ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10245 Vaccinia virus])
 +
}}
 +
 
 +
'''Solution structure of the Z-DNA binding domain of the vaccinia virus gene E3L'''
 +
 
==Overview==
==Overview==
Line 7: Line 16:
==About this Structure==
==About this Structure==
-
1OYI is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Vaccinia_virus Vaccinia virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OYI OCA].
+
1OYI is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Vaccinia_virus Vaccinia virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OYI OCA].
==Reference==
==Reference==
-
The solution structure of the N-terminal domain of E3L shows a tyrosine conformation that may explain its reduced affinity to Z-DNA in vitro., Kahmann JD, Wecking DA, Putter V, Lowenhaupt K, Kim YG, Schmieder P, Oschkinat H, Rich A, Schade M, Proc Natl Acad Sci U S A. 2004 Mar 2;101(9):2712-7. Epub 2004 Feb 23. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=14981270 14981270]
+
The solution structure of the N-terminal domain of E3L shows a tyrosine conformation that may explain its reduced affinity to Z-DNA in vitro., Kahmann JD, Wecking DA, Putter V, Lowenhaupt K, Kim YG, Schmieder P, Oschkinat H, Rich A, Schade M, Proc Natl Acad Sci U S A. 2004 Mar 2;101(9):2712-7. Epub 2004 Feb 23. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/14981270 14981270]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Vaccinia virus]]
[[Category: Vaccinia virus]]
Line 24: Line 33:
[[Category: (alpha+beta) helix-turn-helix]]
[[Category: (alpha+beta) helix-turn-helix]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:23:09 2008''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:17:23 2008''

Revision as of 11:17, 20 March 2008


PDB ID 1oyi

Drag the structure with the mouse to rotate
Gene: E3L (Vaccinia virus)
Coordinates: save as pdb, mmCIF, xml



Solution structure of the Z-DNA binding domain of the vaccinia virus gene E3L


Overview

The N-terminal domain of the vaccinia virus protein E3L (Z alpha(E3L)) is essential for full viral pathogenicity in mice. It has sequence similarity to the high-affinity human Z-DNA-binding domains Z alpha(ADAR1) and Z alpha(DLM1). Here, we report the solution structure of Z alpha(E3L) and the chemical shift map of its interaction surface with Z-DNA. The global structure and the Z-DNA interaction surface of Z alpha(E3L) are very similar to the high-affinity Z-DNA-binding domains Z alpha(ADAR1) and Z alpha(DLM1). However, the key Z-DNA contacting residue Y48 of Z alpha(E3L) adopts a different side chain conformation in unbound Z alpha(E3L), which requires rearrangement for binding to Z-DNA. This difference suggests a molecular basis for the significantly lower in vitro affinity of Z alpha(E3L) to Z-DNA compared with its homologues.

About this Structure

1OYI is a Single protein structure of sequence from Vaccinia virus. Full crystallographic information is available from OCA.

Reference

The solution structure of the N-terminal domain of E3L shows a tyrosine conformation that may explain its reduced affinity to Z-DNA in vitro., Kahmann JD, Wecking DA, Putter V, Lowenhaupt K, Kim YG, Schmieder P, Oschkinat H, Rich A, Schade M, Proc Natl Acad Sci U S A. 2004 Mar 2;101(9):2712-7. Epub 2004 Feb 23. PMID:14981270

Page seeded by OCA on Thu Mar 20 13:17:23 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools