1D2Y

N-TERMINAL DOMAIN CORE METHIONINE MUTATION

Summary for 1D2Y

• Entry DOI: 10.2210/pdb1d2y/pdb
• Related: 1CTW 1CU0 1CU2 1CU3 1CU5 1CU6 1CUP 1CUQ 1CV0 1CV1 1CV3 1CV4 1CV5 1CV6 1CVK 1D2W 1D2Y 1D3F 1D3J 1QSQ
• Descriptor: LYSOZYME, CHLORIDE ION, 2-HYDROXYETHYL DISULFIDE, ... (4 entities in total)
• Functional Keywords: hydrolase (o-glycosyl), t4 lysozyme, methionine core mutant, protein engineering, protein folding, hydrolase
• Biological source: Enterobacteria phage T4
• Cellular location: Host cytoplasm : P00720
• Total number of polymer chains: 1
• Total formula weight: 18871.56

Authors

Gassner, N.C.,Matthews, B.W. (deposition date: 1999-09-28, release date: 1999-10-08, Last modification date: 2024-02-07)

Primary citation

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

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: 10666571
DOI: 10.1006/jmbi.1999.3220

Experimental method

X-RAY DIFFRACTION (2.06 Å)