126l

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(New page: 200px<br /><applet load="126l" size="450" color="white" frame="true" align="right" spinBox="true" caption="126l, resolution 1.80&Aring;" /> '''THE ENERGETIC COST A...)
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[[Image:126l.jpg|left|200px]]<br /><applet load="126l" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="126l, resolution 1.80&Aring;" />
 
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'''THE ENERGETIC COST AND THE STRUCTURAL CONSEQUENCES OF BURYING A HYDROXYL GROUP WITHIN THE CORE OF A PROTEIN DETERMINED FROM ALA TO SER AND VAL TO THR SUBSTITUTIONS IN T4 LYSOZYME'''<br />
 
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==Overview==
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==THE ENERGETIC COST AND THE STRUCTURAL CONSEQUENCES OF BURYING A HYDROXYL GROUP WITHIN THE CORE OF A PROTEIN DETERMINED FROM ALA TO SER AND VAL TO THR SUBSTITUTIONS IN T4 LYSOZYME==
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In order to determine the thermodynamic cost of introducing a polar group, within the core of a protein, a series of nine Ala--&gt;Ser and 3 Val--&gt;Thr, substitutions was constructed in T4 lysozyme. The sites were all within, alpha-helices but ranged from fully solvent-exposed to totally buried. The, range of destabilization incurred by the Ala--&gt;Ser substitutions was found, to be very similar to that for the Val--&gt;Thr replacements. For the, solvent-exposed and partly exposed sites the destabilization was modest, (approximately less than 0.5 kcal/mol). For the completely buried sites, the destabilization was larger, but variable (approximately 1-3 kcal/mol)., Crystal structure determinations showed that the Ala--&gt;Ser mutant, structures were, in general, very similar to their wild-type counterparts, even though the replacements introduce a hydroxyl group. This is in part, because the introduced serines are all within alpha-helices and at, congested sites can avoid steric clashes with surrounding atoms by making, a hydrogen bond to a backbone carbonyl oxygen in the preceding turn of the, helix. The three substituted threonine side chains essentially superimpose, on their valine counterparts but display somewhat larger conformational, adjustments. The results illustrate how a protein structure will adapt in, different ways to avoid the presence of an unsatisfied hydrogen bond donor, or acceptor. In the most extreme case, Val 149--&gt;Thr, which is also the, most destabilizing variant (delta delta G = 2.8 kcal/mol), a water, molecule is incorporated in the mutant structure in order to provide a, hydrogen-bonding partner. The results are consistent with the view that, many hydrogen bonds within proteins contribute only marginally to, stability but that noncharged polar groups that lack a hydrogen-bonding, partner are very destabilizing (delta delta G approximately greater than 3, kcal/mol). Supportive of other studies, the alpha-helix propensity of, alanine is seen to be higher than that of serine (delta delta G = 0.46 +/-, 0.04 kcal/mol), while threonine and valine are similar in alpha-helix, propensity.
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<StructureSection load='126l' size='340' side='right'caption='[[126l]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[126l]] 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=126L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=126L FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
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<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>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=126l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=126l OCA], [https://pdbe.org/126l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=126l RCSB], [https://www.ebi.ac.uk/pdbsum/126l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=126l ProSAT]</span></td></tr>
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</table>
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== Function ==
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[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>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/26/126l_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=126l ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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126L is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Enterobacteria_phage_t2 Enterobacteria phage t2] 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=126L OCA].
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*[[Lysozyme 3D structures|Lysozyme 3D structures]]
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== References ==
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==Reference==
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<references/>
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Energetic cost and structural consequences of burying a hydroxyl group within the core of a protein determined from Ala--&gt;Ser and Val--&gt;Thr substitutions in T4 lysozyme., Blaber M, Lindstrom JD, Gassner N, Xu J, Heinz DW, Matthews BW, Biochemistry. 1993 Oct 26;32(42):11363-73. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8218201 8218201]
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__TOC__
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[[Category: Enterobacteria phage t2]]
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</StructureSection>
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[[Category: Lysozyme]]
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[[Category: Escherichia virus T4]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Blaber, M.]]
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[[Category: Blaber M]]
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[[Category: Matthews, B.W.]]
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[[Category: Matthews BW]]
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[[Category: BME]]
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[[Category: CL]]
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[[Category: hydrolase(o-glycosyl)]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 10:26:10 2007''
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Current revision

THE ENERGETIC COST AND THE STRUCTURAL CONSEQUENCES OF BURYING A HYDROXYL GROUP WITHIN THE CORE OF A PROTEIN DETERMINED FROM ALA TO SER AND VAL TO THR SUBSTITUTIONS IN T4 LYSOZYME

PDB ID 126l

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