2b70

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|GENE= E ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10665 Enterobacteria phage T4])
|GENE= E ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10665 Enterobacteria phage T4])
|DOMAIN=<span class='plainlinks'>[http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=cd00735 bacteriophage_T4-like_lysozyme]</span>
|DOMAIN=<span class='plainlinks'>[http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=cd00735 bacteriophage_T4-like_lysozyme]</span>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2b70 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2b70 OCA], [http://www.ebi.ac.uk/pdbsum/2b70 PDBsum], [http://www.fli-leibniz.de/cgi-bin/ImgLib.pl?CODE=1kfv JenaLib], [http://www.rcsb.org/pdb/explore.do?structureId=2b70 RCSB]</span>
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|RELATEDENTRY=[[2b6t|2B6T]], [[2b6w|2B6W]], [[2b6x|2B6X]], [[2b6y|2B6Y]], [[2b6z|2B6Z]], [[2b72|2B72]], [[2b73|2B73]], [[2b74|2B74]], [[2b75|2B75]]
 +
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2b70 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2b70 OCA], [http://www.ebi.ac.uk/pdbsum/2b70 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2b70 RCSB]</span>
}}
}}
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[[Category: tbsgc]]
[[Category: tbsgc]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Mar 26 06:22:03 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:02:16 2008''

Revision as of 23:02, 30 March 2008

Image:2b70.gif


PDB ID 2b70

Drag the structure with the mouse to rotate
, resolution 2.40Å
Ligands: ,
Gene: E (Enterobacteria phage T4)
Activity: Lysozyme, with EC number 3.2.1.17
Domains: bacteriophage_T4-like_lysozyme
Related: 2B6T, 2B6W, 2B6X, 2B6Y, 2B6Z, 2B72, 2B73, 2B74, 2B75


Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



T4 Lysozyme mutant L99A at ambient pressure


Overview

Formation of a water-expelling nonpolar core is the paradigm of protein folding and stability. Although experiment largely confirms this picture, water buried in "hydrophobic" cavities is required for the function of some proteins. Hydration of the protein core has also been suggested as the mechanism of pressure-induced unfolding. We therefore are led to ask whether even the most nonpolar protein core is truly hydrophobic (i.e., water-repelling). To answer this question we probed the hydration of an approximately 160-A(3), highly hydrophobic cavity created by mutation in T4 lysozyme by using high-pressure crystallography and molecular dynamics simulation. We show that application of modest pressure causes approximately four water molecules to enter the cavity while the protein itself remains essentially unchanged. The highly cooperative filling is primarily due to a small change in bulk water activity, which implies that changing solvent conditions or, equivalently, cavity polarity can dramatically affect interior hydration of proteins and thereby influence both protein activity and folding.

About this Structure

2B70 is a Single protein structure of sequence from Enterobacteria phage t4. Full crystallographic information is available from OCA.

Reference

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

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