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1l79

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[[Image:1l79.jpg|left|200px]]
 
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{{Structure
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==DESIGN AND STRUCTURAL ANALYSIS OF ALTERNATIVE HYDROPHOBIC CORE PACKING ARRANGEMENTS IN BACTERIOPHAGE T4 LYSOZYME==
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|PDB= 1l79 |SIZE=350|CAPTION= <scene name='initialview01'>1l79</scene>, resolution 1.9&Aring;
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<StructureSection load='1l79' size='340' side='right'caption='[[1l79]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene> and <scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>
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<table><tr><td colspan='2'>[[1l79]] 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=1L79 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1L79 FirstGlance]. <br>
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|ACTIVITY= [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]
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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]] 1.9&#8491;</td></tr>
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|GENE=
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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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}}
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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=1l79 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1l79 OCA], [https://pdbe.org/1l79 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1l79 RCSB], [https://www.ebi.ac.uk/pdbsum/1l79 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1l79 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/l7/1l79_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=1l79 ConSurf].
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<div style="clear:both"></div>
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'''DESIGN AND STRUCTURAL ANALYSIS OF ALTERNATIVE HYDROPHOBIC CORE PACKING ARRANGEMENTS IN BACTERIOPHAGE T4 LYSOZYME'''
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==See Also==
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*[[Lysozyme 3D structures|Lysozyme 3D structures]]
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== References ==
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==Overview==
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<references/>
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An attempt has been made to design modified core-packing arrangements in bacteriophage T4 lysozyme. Alternative replacements of the buried residues Leu99, Met102, Val111 and Phe153 were selected using packing calculations and energy minimization. To test the design procedure, a series of multiple mutants was constructed culminating in the replacement L99F/M102L/V111I/F153L. These variants decrease the stability of T4 lysozyme by approximately 0 to 2 kcal/mol. The crystal structures of a number of the variants were determined. In the variant in which Val111 was replaced by Ile, alpha-helix 107-114 moved by approximately 1.5 A, breaking the hydrogen bond between the backbone carbonyl group of Thr109 and the backbone amide group of Gly113. This conformational change was not anticipated by the design procedure. Compensating interactions of magnitude up to 1.1 kcal/mol occur for some sets of mutations, while other sets display nearly additive stability changes. Within experimental error, the stability of the double mutant V111F/F153L is additive, with delta delta G different by only 0.1 kcal/mol from the sum of the two single mutants. The quadruple mutant L99F/M102L/V111I/F153L is destabilized by 0.5 kcal/mol, compared to delta delta G = -1.6 kcal/mol for the sum of the four single mutants. Multiple mutants show smaller overall structural changes from wild-type than M102L or V111I alone. Co-operative changes in structure and stability can be rationalized in terms of specific structural differences between single and multiple mutants. Genuine repacking of the hydrophobic core of T4 lysozyme with minimal effects on structure, stability and activity thus appears to have been achieved.
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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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1L79 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Enterobacteria_phage_t2 Enterobacteria phage t2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1L79 OCA].
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[[Category: Large Structures]]
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[[Category: Hurley JH]]
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==Reference==
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[[Category: Matthews BW]]
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Design and structural analysis of alternative hydrophobic core packing arrangements in bacteriophage T4 lysozyme., Hurley JH, Baase WA, Matthews BW, J Mol Biol. 1992 Apr 20;224(4):1143-59. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/1569571 1569571]
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[[Category: Enterobacteria phage t2]]
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[[Category: Lysozyme]]
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[[Category: Single protein]]
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[[Category: Hurley, J H.]]
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[[Category: Matthews, B W.]]
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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://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:27:24 2008''
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Current revision

DESIGN AND STRUCTURAL ANALYSIS OF ALTERNATIVE HYDROPHOBIC CORE PACKING ARRANGEMENTS IN BACTERIOPHAGE T4 LYSOZYME

PDB ID 1l79

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