1L84

A CAVITY-CONTAINING MUTANT OF T4 LYSOZYME IS STABILIZED BY BURIED BENZENE

Summary for 1L84

• Entry DOI: 10.2210/pdb1l84/pdb
• Descriptor: T4 LYSOZYME, CHLORIDE ION, BETA-MERCAPTOETHANOL, ... (5 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: 18815.47

Authors

Eriksson, A.E.,Matthews, B.W. (deposition date: 1992-01-21, release date: 1993-10-31, Last modification date: 2024-02-14)

Primary citation

Eriksson, A.E.,Baase, W.A.,Wozniak, J.A.,Matthews, B.W.
A cavity-containing mutant of T4 lysozyme is stabilized by buried benzene.
Nature, 355:371-373, 1992

PubMed Abstract: The hydrophobic cores of proteins are generally well packed, with few cavities. Mutations in which a bulky buried residue such as leucine or phenylalanine is replaced with a small residue such as alanine can create cavities in the core of a protein (our unpublished results). The sizes and shapes of such cavities can vary substantially depending on factors such as local geometry, whether or not a cavity already exists at the site of substitution, and the degree to which the protein structure relaxes to occupy the space vacated by the substituted residue. We show by crystallographic and thermodynamic analysis that the cavity created by the replacement Leu 99----Ala in T4 lysozyme is large enough to bind benzene and that ligand binding increases the melting temperature of the protein by 6.0 degrees C at pH 3.0. Benzene does not, however, bind to the cavity created by the Phe 153----Ala replacement. The results show that cavities can be engineered in proteins and suggest that such cavities might be tailored to bind specific ligands. The binding of benzene at an internal site 7 A from the molecular surface also illustrates the dynamic nature of proteins, even in crystals.

PubMed: 1731252
DOI: 10.1038/355371a0

Experimental method

X-RAY DIFFRACTION (1.9 Å)