1CX6

T4 LYSOZYME SUBSTITUTED WITH SELENOMETHIONINE

1CX6 の概要

• エントリーDOI: 10.2210/pdb1cx6/pdb
• 分子名称: LYSOZYME, CHLORIDE ION, 2-HYDROXYETHYL DISULFIDE, ... (4 entities in total)
• 機能のキーワード: hydrolase (o-glycosyl), t4 lysozyme, selenomethionine core mutant, protein engineering, protein folding, 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: 19508.51

構造登録者

Gassner, N.C.,Baase, W.A.,Matthews, B.W. (登録日: 1999-08-28, 公開日: 1999-12-15, 最終更新日: 2024-10-30)

主引用文献

Gassner, N.C.,Baase, W.A.,Hausrath, A.C.,Matthews, B.W.
Substitution with selenomethionine can enhance the stability of methionine-rich proteins.
J.Mol.Biol., 294:17-20, 1999

PubMed Abstract: The availability of a series of phage T4 lysozymes with up to 14 methionine residues incorporated within the protein has made it possible to systematically compare the effect on protein stability of selenomethionine relative to methionine. Wild-type lysozyme contains two fully buried methionine residues plus three more on the surface. The substitution of these methionine residues with selenomethionine slightly stabilizes the protein. As more and more methionine residues are substituted into the protein, there is a progressive loss of stability. This is, however, increasingly offset in the selenomethionine variants, ultimately resulting in a differential increase in melting temperature of about 7 degrees C. This increase, corresponding to about 0.25 kcal/mol per substitution, is in reasonable agreement with the difference in the solvent transfer free energy between the two amino acids.

PubMed: 10556025
DOI: 10.1006/jmbi.1999.3220

実験手法

X-RAY DIFFRACTION (2.01 Å)