2aud
From Proteopedia
Unliganded HincII
Overview
The 2.1A crystal structure of the unliganded type II restriction endonuclease, HincII, is described. Although the asymmetric unit contains only a single monomer, crystal lattice contacts bring two monomers together to form a dimer very similar to that found in the DNA bound form. Comparison with the published DNA bound structure reveals that the DNA binding pocket is expanded in the unliganded structure. Comparison of the unliganded and DNA liganded structures reveals a simple rotation of subunits by 11 degrees each, or 22 degrees total, to a more closed structure around the bound DNA. Comparison of this conformational change to that observed in the other type II restriction endonucleases where DNA bound and unliganded forms have both been characterized, shows considerable variation in the types of conformational changes that can occur. The conformational changes in three can be described by a simple rotation of subunits, while in two others both rotation and translation of subunits relative to one another occurs. In addition, the endonucleases having subunits that undergo the greatest amount of rotation upon DNA binding are found to be those that distort the bound DNA the least, suggesting that DNA bending may be less facile in dimers possessing greater flexibility.
About this Structure
2AUD is a Single protein structure of sequence from Haemophilus influenzae. Full crystallographic information is available from OCA.
Reference
DNA-induced conformational changes in type II restriction endonucleases: the structure of unliganded HincII., Little EJ, Horton NC, J Mol Biol. 2005 Aug 5;351(1):76-88. PMID:15993893 Page seeded by OCA on Sat May 3 19:29:18 2008
