2oe9: Difference between revisions

Revision as of 04:13, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2oe9.png

Template:STRUCTURE 2oe9

High-pressure structure of pseudo-WT T4 LysozymeHigh-pressure structure of pseudo-WT T4 Lysozyme

Template:ABSTRACT PUBMED 17292912

About this StructureAbout this Structure

2OE9 is a Single protein structure of sequence from Enterobacteria phage t4. 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

Cooperative water filling of a nonpolar protein cavity observed by high-pressure crystallography and simulation., Collins MD, Hummer G, Quillin ML, Matthews BW, Gruner SM, Proc Natl Acad Sci U S A. 2005 Nov 15;102(46):16668-71. Epub 2005 Nov 3. PMID:16269539

Page seeded by OCA on Mon Jul 28 04:13:14 2008

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OCA

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-[[Image:2oe9.gif|left|200px]]
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 {{STRUCTURE_2oe9|  PDB=2oe9  |  SCENE=  }}
-'''High-pressure structure of pseudo-WT T4 Lysozyme'''
+===High-pressure structure of pseudo-WT T4 Lysozyme===
-==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.
+The line below this paragraph, {{ABSTRACT_PUBMED_17292912}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 17292912 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_17292912}}
 ==About this Structure==
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 ==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://www.ncbi.nlm.nih.gov/pubmed/17292912 17292912]
+Cooperative water filling of a nonpolar protein cavity observed by high-pressure crystallography and simulation., Collins MD, Hummer G, Quillin ML, Matthews BW, Gruner SM, Proc Natl Acad Sci U S A. 2005 Nov 15;102(46):16668-71. Epub 2005 Nov 3. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16269539 16269539]
 [[Category: Enterobacteria phage t4]]
 [[Category: Lysozyme]]
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 [[Category: High-pressure]]
 [[Category: T4 lysozyme]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 10:43:42 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 04:13:14 2008''