1l84
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(New page: 200px<br /><applet load="1l84" size="450" color="white" frame="true" align="right" spinBox="true" caption="1l84, resolution 1.90Å" /> '''A CAVITY-CONTAINING ...)
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Revision as of 18:14, 20 November 2007
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A CAVITY-CONTAINING MUTANT OF T4 LYSOZYME IS STABILIZED BY BURIED BENZENE
Overview
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or, phenylalanine is replaced with a small residue such as alanine can create, cavities in the core of a protein (our unpublished results).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.
About this Structure
1L84 is a Single protein structure of sequence from Enterobacteria phage t2 with CL, BME and BNZ as ligands. Active as Lysozyme, with EC number 3.2.1.17 Full crystallographic information is available from OCA.
Reference
A cavity-containing mutant of T4 lysozyme is stabilized by buried benzene., Eriksson AE, Baase WA, Wozniak JA, Matthews BW, Nature. 1992 Jan 23;355(6358):371-3. PMID:1731252
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