2AUD

Unliganded HincII

2AUD の概要

• エントリーDOI: 10.2210/pdb2aud/pdb
• 分子名称: Type II restriction enzyme HincII (2 entities in total)
• 機能のキーワード: restriction endonuclease, dna binding, blunt cutter, hydrolase
• 由来する生物種: Haemophilus influenzae
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 29835.08

構造登録者

Horton, N.C.,Little, E.J. (登録日: 2005-08-27, 公開日: 2005-10-04, 最終更新日: 2023-08-23)

主引用文献

Horton, N.C.,Little, E.J.
DNA-induced conformational changes in Type II restriction endonucleases: The structure of unliganded HincII
J.Mol.Biol., 351:76-88, 2005

PubMed Abstract: 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.

PubMed: 15993893
DOI: 10.1016/j.jmb.2005.05.063

実験手法

X-RAY DIFFRACTION (2.1 Å)