2oe9: Difference between revisions

Revision as of 19:17, 21 February 2008

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

2OE9 is a Single protein structure of sequence from Bacteriophage t4 with and 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

Page seeded by OCA on Thu Feb 21 18:17:27 2008

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OCA

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-[[Image:2oe9.gif|left|200px]]<br /><applet load="2oe9" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:2oe9.gif|left|200px]]<br /><applet load="2oe9" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="2oe9, resolution 2.010&Aring;" />
 '''High-pressure structure of pseudo-WT T4 Lysozyme'''<br />
 ==Overview==
-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.
+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 Structure==
-OE9 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacteriophage_t4 Bacteriophage t4] with CL and BME as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Lysozyme Lysozyme], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.17 3.2.1.17] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2OE9 OCA].
+OE9 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacteriophage_t4 Bacteriophage t4] with <scene name='pdbligand=CL:'>CL</scene> and <scene name='pdbligand=BME:'>BME</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Lysozyme Lysozyme], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.17 3.2.1.17] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OE9 OCA].
 ==Reference==
-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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17292912 17292912]
+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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17292912 17292912]
 [[Category: Bacteriophage t4]]
 [[Category: Lysozyme]]
 [[Category: Single protein]]
-[[Category: Collins, M.D.]]
+[[Category: Collins, M D.]]
-[[Category: Gruner, S.M.]]
+[[Category: Gruner, S M.]]
-[[Category: Matthews, B.W.]]
+[[Category: Matthews, B W.]]
-[[Category: Quillin, M.L.]]
+[[Category: Quillin, M L.]]
 [[Category: BME]]
 [[Category: CL]]
@@ Line 23: / Line 23: @@
 [[Category: t4 lysozyme]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 13:08:37 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:17:27 2008''