1l24

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{{Seed}}
 
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[[Image:1l24.png|left|200px]]
 
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==ENHANCED PROTEIN THERMOSTABILITY FROM SITE-DIRECTED MUTATIONS THAT DECREASE THE ENTROPY OF UNFOLDING==
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The line below this paragraph, containing "STRUCTURE_1l24", creates the "Structure Box" on the page.
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<StructureSection load='1l24' size='340' side='right'caption='[[1l24]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1l24]] 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=1L24 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1L24 FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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]] 1.7&#8491;</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=1l24 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1l24 OCA], [https://pdbe.org/1l24 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1l24 RCSB], [https://www.ebi.ac.uk/pdbsum/1l24 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1l24 ProSAT]</span></td></tr>
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{{STRUCTURE_1l24| PDB=1l24 | SCENE= }}
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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/l2/1l24_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=1l24 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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It is proposed that the stability of a protein can be increased by selected amino acid substitutions that decrease the configurational entropy of unfolding. Two such substitutions, one of the form Xaa----Pro and the other of the form Gly----Xaa, were constructed in bacteriophage T4 lysozyme at sites consistent with the known three-dimensional structure. Both substitutions stabilize the protein toward reversible and irreversible thermal denaturation at physiological pH. The substitutions have no effect on enzymatic activity. High-resolution crystallographic analysis of the proline-containing mutant protein (Ala-82----Pro) shows that its three-dimensional structure is essentially identical with the wild-type enzyme. The overall structure of the other mutant enzyme (Gly-77----Ala) is also very similar to wild-type lysozyme, although there are localized conformational adjustments in the vicinity of the altered amino acid. The combination of a number of such amino acid replacements, each of which is expected to contribute approximately 1 kcal/mol (1 cal = 4.184 J) to the free energy of folding, may provide a general strategy for substantial improvement in the stability of a protein.
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===ENHANCED PROTEIN THERMOSTABILITY FROM SITE-DIRECTED MUTATIONS THAT DECREASE THE ENTROPY OF UNFOLDING===
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Enhanced protein thermostability from site-directed mutations that decrease the entropy of unfolding.,Matthews BW, Nicholson H, Becktel WJ Proc Natl Acad Sci U S A. 1987 Oct;84(19):6663-7. PMID:3477797<ref>PMID:3477797</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1l24" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_3477797}}, adds the Publication Abstract to the page
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*[[Lysozyme 3D structures|Lysozyme 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 3477797 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_3477797}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Escherichia virus T4]]
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1L24 is a 1 chain structure with 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=1L24 OCA].
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[[Category: Large Structures]]
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[[Category: Matthews BW]]
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==Reference==
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[[Category: Nicholson H]]
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<ref group="xtra">PMID:3477797</ref><references group="xtra"/>
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[[Category: Enterobacteria phage t4]]
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[[Category: Lysozyme]]
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[[Category: Matthews, B W.]]
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[[Category: Nicholson, H.]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Mar 3 14:07:30 2010''
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Current revision

ENHANCED PROTEIN THERMOSTABILITY FROM SITE-DIRECTED MUTATIONS THAT DECREASE THE ENTROPY OF UNFOLDING

PDB ID 1l24

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