2oea: Difference between revisions

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[[Image:2oea.gif|left|200px]]
[[Image:2oea.gif|left|200px]]


{{Structure
<!--
|PDB= 2oea |SIZE=350|CAPTION= <scene name='initialview01'>2oea</scene>, resolution 2.010&Aring;
The line below this paragraph, containing "STRUCTURE_2oea", creates the "Structure Box" on the page.
|SITE=
You may change the PDB parameter (which sets the PDB file loaded into the applet)  
|LIGAND= <scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
|ACTIVITY= <span class='plainlinks'>[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] </span>
or leave the SCENE parameter empty for the default display.
|GENE= E ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10665 Enterobacteria phage T4])
-->
|DOMAIN=
{{STRUCTURE_2oea|  PDB=2oea |  SCENE= }}  
|RELATEDENTRY=[[2b6t|2B6T]], [[2oe4|2OE4]], [[2oe7|2OE7]], [[2oe9|2OE9]]
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2oea FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2oea OCA], [http://www.ebi.ac.uk/pdbsum/2oea PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2oea RCSB]</span>
}}


'''High-pressure structure of pseudo-WT T4 Lysozyme'''
'''High-pressure structure of pseudo-WT T4 Lysozyme'''
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[[Category: Matthews, B W.]]
[[Category: Matthews, B W.]]
[[Category: Quillin, M L.]]
[[Category: Quillin, M L.]]
[[Category: high-pressure]]
[[Category: High-pressure]]
[[Category: t4 lysozyme]]
[[Category: T4 lysozyme]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 10:43:45 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:16:32 2008''

Revision as of 10:43, 4 May 2008

File:2oea.gif

Template:STRUCTURE 2oea

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 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 Page seeded by OCA on Sun May 4 10:43:45 2008

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