256L

BACTERIOPHAGE T4 LYSOZYME

256L の概要

• エントリーDOI: 10.2210/pdb256l/pdb
• 分子名称: LYSOZYME (2 entities in total)
• 機能のキーワード: lysozyme, hydrolase
• 由来する生物種: Enterobacteria phage T4
• 細胞内の位置: Host cytoplasm : P00720
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 18644.43

構造登録者

Faber, H.R.,Matthews, B.W. (登録日: 1998-02-24, 公開日: 1998-05-27, 最終更新日: 2024-04-03)

主引用文献

Faber, H.R.,Matthews, B.W.
A mutant T4 lysozyme displays five different crystal conformations.
Nature, 348:263-266, 1990

PubMed Abstract: Phage T4 lysozyme consists of two domains between which is formed the active-site cleft of the enzyme. The crystallographically determined thermal displacement parameters for the protein suggested that the amino terminal of the two domains undergoes 'hinge-bending' motion about an axis passing through the waist of the molecule. Such conformational mobility may be important in allowing access of substrates to the active site of the enzyme. We report here a crystallographic study of a mutant T4 lysozyme which demonstrates further the conformational flexibility of the protein. A mutant form of the enzyme with a methionine residue (Met 6) replaced by isoleucine crystallizes with four independent molecules in the crystal lattice. These four molecules have distinctly different conformations. The mutant protein can also crystallize in standard form with a structure very similar to the wild-type protein. Thus the mutant protein can adopt five different crystal conformations. The isoleucine for methionine substitution at the intersection of the two domains of T4 lysozyme apparently enhances the hinge-bending motion presumed to occur in the wild-type protein, without significantly affecting the catalytic activity or thermal stability of the protein.

PubMed: 2234094
DOI: 10.1038/348263a0

実験手法

X-RAY DIFFRACTION (1.8 Å)