1CX6
T4 LYSOZYME SUBSTITUTED WITH SELENOMETHIONINE
Summary for 1CX6
| Entry DOI | 10.2210/pdb1cx6/pdb |
| Descriptor | LYSOZYME, CHLORIDE ION, 2-HYDROXYETHYL DISULFIDE, ... (4 entities in total) |
| Functional Keywords | hydrolase (o-glycosyl), t4 lysozyme, selenomethionine 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 | 19508.51 |
| Authors | Gassner, N.C.,Baase, W.A.,Matthews, B.W. (deposition date: 1999-08-28, release date: 1999-12-15, Last modification date: 2024-10-30) |
| Primary citation | 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 Cited by 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: 10556025DOI: 10.1006/jmbi.1999.3220 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.01 Å) |
Structure validation
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