1e7l

From Proteopedia

Revision as of 13:02, 30 October 2007

ENDONUCLEASE VII (ENDOVII) N62D MUTANT FROM PHAGE T4

Overview

The structure of the N62D mutant of the junction-resolving endonuclease, VII (EndoVII) from phage T4 has been refined at 1.3 A, and a second, wild-type crystal form solved and refined at 2.8 A resolution. Comparison, of the mutant with the wild-type protein structure in two different, crystal environments reveals considerable conformational flexibility at, the dimer level affecting the substrate-binding cleft, the dimerization, interface and the orientation of the C-terminal domains. The opening of, the DNA-binding cleft, the orientation of the C-terminal domains relative, to the central dimerization domain as well as the relative positioning of, helices in the dimerization interface appear to be sensitive to the, crystal packing environment. The highly unexpected rearrangement within, ... [(full description)]

About this Structure

1E7L is a [Single protein] structure of sequence from [Enterobacteria phage t2] with SO4 and ZN as [ligands]. Structure known Active Sites: A, B, ZN1 and ZN2. Full crystallographic information is available from [OCA].

Reference

Conformational flexibility in T4 endonuclease VII revealed by crystallography: implications for substrate binding and cleavage., Raaijmakers H, Toro I, Birkenbihl R, Kemper B, Suck D, J Mol Biol. 2001 Apr 27;308(2):311-23. PMID:11327769

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