1T8F

Crystal structure of phage T4 lysozyme mutant R14A/K16A/I17A/K19A/T21A/E22A/C54T/C97A

Summary for 1T8F

• Entry DOI: 10.2210/pdb1t8f/pdb
• Descriptor: Lysozyme, CHLORIDE ION, BETA-MERCAPTOETHANOL, ... (4 entities in total)
• Functional Keywords: poly-alanine mutation, t4, lysozyme, hydrolase
• Biological source: Enterobacteria phage T4
• Total number of polymer chains: 1
• Total formula weight: 18523.07

Authors

He, M.M.,Wood, Z.A.,Baase, W.A.,Xiao, H.,Matthews, B.W. (deposition date: 2004-05-12, release date: 2004-10-19, Last modification date: 2024-02-14)

Primary citation

He, M.M.,Wood, Z.A.,Baase, W.A.,Xiao, H.,Matthews, B.W.
Alanine-scanning mutagenesis of the beta-sheet region of phage T4 lysozyme suggests that tertiary context has a dominant effect on beta-sheet formation.
Protein Sci., 13:2716-2724, 2004

PubMed Abstract: In general, alpha-helical conformations in proteins depend in large part on the amino acid residues within the helix and their proximal interactions. For example, an alanine residue has a high propensity to adopt an alpha-helical conformation, whereas that of a glycine residue is low. The sequence preferences for beta-sheet formation are less obvious. To identify the factors that influence beta-sheet conformation, a series of scanning polyalanine mutations were made within the strands and associated turns of the beta-sheet region in T4 lysozyme. For each construct the stability of the folded protein was reduced substantially, consistent with removal of native packing interactions. However, the crystal structures showed that each of the mutants retained the beta-sheet conformation. These results suggest that the structure of the beta-sheet region of T4 lysozyme is maintained to a substantial extent by tertiary interactions with the surrounding parts of the protein. Such tertiary interactions may be important in determining the structures of beta-sheets in general.

PubMed: 15340171
DOI: 10.1110/ps.04875504

Experimental method

X-RAY DIFFRACTION (2.15 Å)