1OYI

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

Summary for 1OYI

• Entry DOI: 10.2210/pdb1oyi/pdb
• Descriptor: double-stranded RNA-binding protein (1 entity in total)
• Functional Keywords: (alpha+beta) helix-turn-helix, viral protein
• Biological source: Vaccinia virus
• Total number of polymer chains: 1
• Total formula weight: 9192.25

Authors

Kahmann, J.D.,Wecking, D.A.,Putter, V.,Lowenhaupt, K.,Kim, Y.-G.,Schmieder, P.,Oschkinat, H.,Rich, A.,Schade, M. (deposition date: 2003-04-04, release date: 2004-03-09, Last modification date: 2024-05-22)

Primary citation

Kahmann, J.D.,Wecking, D.A.,Putter, V.,Lowenhaupt, K.,Kim, Y.-G.,Schmieder, P.,Oschkinat, H.,Rich, A.,Schade, M.
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.
Proc.Natl.Acad.Sci.USA, 101:2712-2717, 2004

PubMed Abstract: 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.

PubMed: 14981270
DOI: 10.1073/pnas.0308612100

Experimental method

SOLUTION NMR