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[[Image:2b6x.gif|left|200px]]


{{Structure
==T4 Lysozyme mutant L99A at 200 MPa==
|PDB= 2b6x |SIZE=350|CAPTION= <scene name='initialview01'>2b6x</scene>, resolution 2.107&Aring;
<StructureSection load='2b6x' size='340' side='right'caption='[[2b6x]], [[Resolution|resolution]] 2.11&Aring;' scene=''>
|SITE=
== Structural highlights ==
|LIGAND= <scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>
<table><tr><td colspan='2'>[[2b6x]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_virus_T4 Escherichia virus T4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2B6X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2B6X FirstGlance]. <br>
|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>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.107&#8491;</td></tr>
|GENE=  
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr>
|DOMAIN=
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2b6x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2b6x OCA], [https://pdbe.org/2b6x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2b6x RCSB], [https://www.ebi.ac.uk/pdbsum/2b6x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2b6x ProSAT]</span></td></tr>
|RELATEDENTRY=[[2b6t|2B6T]], [[2b6w|2B6W]], [[2b6y|2B6Y]], [[2b6z|2B6Z]], [[2b70|2B70]], [[2b72|2B72]], [[2b73|2B73]], [[2b74|2B74]], [[2b75|2B75]]
</table>
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2b6x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2b6x OCA], [http://www.ebi.ac.uk/pdbsum/2b6x PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2b6x RCSB]</span>
== Function ==
}}
[https://www.uniprot.org/uniprot/ENLYS_BPT4 ENLYS_BPT4] Endolysin with lysozyme activity that degrades host peptidoglycans and participates with the holin and spanin proteins in the sequential events which lead to the programmed host cell lysis releasing the mature viral particles. Once the holin has permeabilized the host cell membrane, the endolysin can reach the periplasm and break down the peptidoglycan layer.<ref>PMID:22389108</ref>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/b6/2b6x_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2b6x ConSurf].
<div style="clear:both"></div>


'''T4 Lysozyme mutant L99A at 200 MPa'''
==See Also==
 
*[[Lysozyme 3D structures|Lysozyme 3D structures]]
 
== References ==
==Overview==
<references/>
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.
__TOC__
 
</StructureSection>
==About this Structure==
[[Category: Escherichia virus T4]]
2B6X is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Enterobacteria_phage_t4 Enterobacteria phage t4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2B6X OCA].
[[Category: Large Structures]]
 
[[Category: Collins MD]]
==Reference==
[[Category: Gruner SM]]
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: Matthews BW]]
[[Category: Enterobacteria phage t4]]
[[Category: Quillin ML]]
[[Category: Lysozyme]]
[[Category: Single protein]]
[[Category: Collins, M D.]]
[[Category: Gruner, S M.]]
[[Category: Matthews, B W.]]
[[Category: Quillin, M L.]]
[[Category: high pressure]]
[[Category: t4 lysozyme]]
 
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