1oyi
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(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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Revision as of 23:33, 24 November 2007
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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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