1l60

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(New page: 200px<br /><applet load="1l60" size="450" color="white" frame="true" align="right" spinBox="true" caption="1l60, resolution 1.7&Aring;" /> '''ANALYSIS OF THE INTER...)
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[[Image:1l60.gif|left|200px]]<br /><applet load="1l60" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1l60, resolution 1.7&Aring;" />
 
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'''ANALYSIS OF THE INTERACTION BETWEEN CHARGED SIDE CHAINS AND THE ALPHA-HELIX DIPOLE USING DESIGNED THERMOSTABLE MUTANTS OF PHAGE T4 LYSOZYME'''<br />
 
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==Overview==
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==ANALYSIS OF THE INTERACTION BETWEEN CHARGED SIDE CHAINS AND THE ALPHA-HELIX DIPOLE USING DESIGNED THERMOSTABLE MUTANTS OF PHAGE T4 LYSOZYME==
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It was previously shown that the two replacements Gly 77--&gt;Ala (G77A) and, Ala 82--&gt;Pro (A82P) increase the thermostability of phage T4 lysozyme at, pH 6.5. Such replacements are presumed to restrict the degrees of freedom, of the unfolded protein and so decrease the entropy of unfolding [B. W., Matthews, H. Nicholson, and W. J. Becktel (1987) Proceedings of the, National Academy of Science USA Vol. 84, pp. 6663-6667]. To further test, this approach, three additional replacements--G113A, K60P and A93P--have, been constructed. On the basis of model building, each of these three, replacements was judged to be less than optimal because it would tend to, introduce unfavorable van der Waals contacts with neighboring parts of the, protein. The presence of such contacts was verified for G113A and K60P by, conformational adjustments seen in the crystal structures of these mutant, proteins. In the case of G113A there are backbone conformational changes, of 0.5-1.0 A in the short alpha-helix, 108-113, that includes the site of, substitution. In the case of K60P the pyrrolidine ring shows evidence of, strain. The thermal stability of each of the three variants at both pH 2.0, and pH 6.5 was found to be very close to that of wild-type lysozyme. The, results suggest that the procedure used to predict sites for both, Xaa--&gt;Pro and Gly--&gt;Ala is, in principle, correct. At the same time, the, increase in stability expected from substitutions of this type is modest, and can easily be offset by strain associated with introduction of the, alanine or proline. This means that the criteria used to select, substitutions that will increase thermostability have to be stringent at, least. In the case of T4 lysozyme this severely limits the number of, sites. The analysis reveals a significant discrepancy between the, conformational energy surface predicted for the residue preceding a, proline and the conformations observed in crystal structures.
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<StructureSection load='1l60' size='340' side='right'caption='[[1l60]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1l60]] 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=1L60 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1L60 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]] 1.7&#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=1l60 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1l60 OCA], [https://pdbe.org/1l60 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1l60 RCSB], [https://www.ebi.ac.uk/pdbsum/1l60 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1l60 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/l6/1l60_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=1l60 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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1L60 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacteriophage_t4 Bacteriophage t4]. 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=1L60 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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Analysis of the effectiveness of proline substitutions and glycine replacements in increasing the stability of phage T4 lysozyme., Nicholson H, Tronrud DE, Becktel WJ, Matthews BW, Biopolymers. 1992 Nov;32(11):1431-41. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=1457724 1457724]
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__TOC__
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[[Category: Bacteriophage t4]]
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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: Matthews, B.W.]]
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[[Category: Matthews BW]]
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[[Category: Nicholson, H.]]
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[[Category: Nicholson H]]
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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 20:18:04 2007''
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ANALYSIS OF THE INTERACTION BETWEEN CHARGED SIDE CHAINS AND THE ALPHA-HELIX DIPOLE USING DESIGNED THERMOSTABLE MUTANTS OF PHAGE T4 LYSOZYME

PDB ID 1l60

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