1oyi
From Proteopedia
(New page: 200px<br /><applet load="1oyi" size="450" color="white" frame="true" align="right" spinBox="true" caption="1oyi" /> '''Solution structure of the Z-DNA binding doma...) |
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'''Solution structure of the Z-DNA binding domain of the vaccinia virus gene E3L'''<br /> | '''Solution structure of the Z-DNA binding domain of the vaccinia virus gene E3L'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The N-terminal domain of the vaccinia virus protein E3L (Z alpha(E3L)) is | + | 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== | ==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:// | + | 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]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Vaccinia virus]] | [[Category: Vaccinia virus]] | ||
| - | [[Category: Kahmann, J | + | [[Category: Kahmann, J D.]] |
| - | [[Category: Kim, Y | + | [[Category: Kim, Y G.]] |
[[Category: Lowenhaupt, K.]] | [[Category: Lowenhaupt, K.]] | ||
[[Category: Oschkinat, H.]] | [[Category: Oschkinat, H.]] | ||
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[[Category: Schade, M.]] | [[Category: Schade, M.]] | ||
[[Category: Schmieder, P.]] | [[Category: Schmieder, P.]] | ||
| - | [[Category: Wecking, D | + | [[Category: Wecking, D A.]] |
[[Category: (alpha+beta) helix-turn-helix]] | [[Category: (alpha+beta) helix-turn-helix]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:23:09 2008'' |
Revision as of 12:23, 21 February 2008
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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
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