2oea
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High-pressure structure of pseudo-WT T4 Lysozyme
OverviewOverview
Steric constraints, charged interactions and many other forces important, to protein structure and function can be explored by mutagenic, experiments. Research of this kind has led to a wealth of knowledge about, what stabilizes proteins in their folded states. To gain a more complete, picture requires that we perturb these structures in a continuous manner, something mutagenesis cannot achieve. With high pressure crystallographic, methods it is now possible to explore the detailed properties of proteins, while continuously varying thermodynamic parameters. Here, we detail the, structural response of the cavity-containing mutant L99A of T4 lysozyme, as well as its pseudo wild-type (WT*) counterpart, to hydrostatic, pressure. Surprisingly, the cavity has almost no effect on the pressure, response: virtually the same changes are observed in WT* as in L99A under, pressure. The cavity is most rigid, while other regions deform, substantially. This implies that while some residues may increase the, thermodynamic stability of a protein, they may also be structurally, irrelevant. As recently shown, the cavity fills with water at pressures, above 100 MPa while retaining its overall size. The resultant picture of, the protein is one in which conformationally fluctuating side groups, provide a liquid-like environment, but which also contribute to the, rigidity of the peptide backbone.
About this StructureAbout this Structure
2OEA is a Single protein structure of sequence from Bacteriophage t4 with CL and BME as ligands. Active as Lysozyme, with EC number 3.2.1.17 Full crystallographic information is available from OCA.
ReferenceReference
Structural Rigidity of a Large Cavity-containing Protein Revealed by High-pressure Crystallography., Collins MD, Quillin ML, Hummer G, Matthews BW, Gruner SM, J Mol Biol. 2007 Mar 30;367(3):752-63. Epub 2006 Dec 15. PMID:17292912
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