1D2Y
N-TERMINAL DOMAIN CORE METHIONINE MUTATION
1D2Y の概要
エントリーDOI | 10.2210/pdb1d2y/pdb |
関連するPDBエントリー | 1CTW 1CU0 1CU2 1CU3 1CU5 1CU6 1CUP 1CUQ 1CV0 1CV1 1CV3 1CV4 1CV5 1CV6 1CVK 1D2W 1D2Y 1D3F 1D3J 1QSQ |
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, methionine 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 | 18871.56 |
構造登録者 | |
主引用文献 | Gassner, N.C.,Matthews, B.W. Use of differentially substituted selenomethionine proteins in X-ray structure determination. Acta Crystallogr.,Sect.D, 55:1967-1970, 1999 Cited by PubMed Abstract: Using heavily methionine-substituted T4 lysozyme as an example, it is shown how the addition or deletion of a small number of methionines can simplify the location of selenium sites for use in MAD phasing. By comparing the X-ray data for a large number of singly substituted lysozymes, it is shown that the optimal amino acid to be substituted by methionine is leucine, followed, in order of preference, by phenylalanine, isoleucine and valine. The identification of leucine as the first choice agrees with the ranking suggested by the Dayhoff mutation probability, i.e. by the frequency of amino-acid substitutions in the sequences of related proteins. The ranking of the second and subsequent choices, however, differ significantly. PubMed: 10666571DOI: 10.1006/jmbi.1999.3220 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (2.06 Å) |
構造検証レポート
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