1L20

ENHANCED PROTEIN THERMOSTABILITY FROM DESIGNED MUTATIONS THAT INTERACT WITH ALPHA-HELIX DIPOLES

Summary for 1L20

Entry DOI	10.2210/pdb1l20/pdb
Related	1L01 1L02 1L03 1L04 1L05 1L06 1L07 1L08 1L09 1L10 1L11 1L12 1L13 1L14 1L15 1L16 1L17 1L18 1L19 1L21 1L22 1L23 1L24 1L25 1L26 1L27 1L28 1L29 1L30 1L31 1L32 1L33 1L34 1L35 1L36 2LZM
Descriptor	T4 LYSOZYME (2 entities in total)
Functional Keywords	hydrolase (o-glycosyl)
Biological source	Enterobacteria phage T4
Cellular location	Host cytoplasm : P00720
Total number of polymer chains	1
Total formula weight	18663.45
Authors	Nicholson, H.,Matthews, B.W. (deposition date: 1989-05-01, release date: 1990-01-15, Last modification date: 2024-05-22)
Primary citation	Nicholson, H.,Becktel, W.J.,Matthews, B.W. Enhanced protein thermostability from designed mutations that interact with alpha-helix dipoles. Nature, 336:651-656, 1988 Cited by PubMed Abstract: Two different genetically engineered amino-acid substitutions designed to interact with alpha-helix dipoles in T4 lysozyme are shown to increase the thermal stability of the protein. Crystallographic analyses of the mutant lysozyme structures suggest that the stabilization is due to electrostatic interaction and does not require precise hydrogen bonding between the substituted amino acid and the end of the alpha-helix. PubMed: 3200317 DOI: 10.1038/336651a0 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.85 Å)

Structure validation