1D3N

METHIONINE CORE MUTATION

Summary for 1D3N

• Entry DOI: 10.2210/pdb1d3n/pdb
• Related: 1cx6 1cx7 1D3M 1D3N
• Descriptor: LYSOZYME, CHLORIDE ION, 2-HYDROXYETHYL DISULFIDE, ... (4 entities in total)
• Functional Keywords: hydrolase (o-glycosyl), t4 lysozyme, methionine core mutant, selenomethionine, protein engineering, protein folding, hydrolase
• Biological source: Enterobacteria phage T4
• Cellular location: Host cytoplasm : P00720
• Total number of polymer chains: 1
• Total formula weight: 19412.67

Authors

Gassner, N.C.,Matthews, B.W. (deposition date: 1999-09-29, release date: 1999-09-30, Last modification date: 2024-10-30)

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 Å)