1l76

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[[Image:1l76.jpg|left|200px]]
 
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{{Structure
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==TOLERANCE OF T4 LYSOZYME TO PROLINE SUBSTITUTIONS WITHIN THE LONG INTERDOMAIN ALPHA-HELIX ILLUSTRATES THE ADAPTABILITY OF PROTEINS TO POTENTIALLY DESTABILIZING LESIONS==
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|PDB= 1l76 |SIZE=350|CAPTION= <scene name='initialview01'>1l76</scene>, resolution 1.9&Aring;
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<StructureSection load='1l76' size='340' side='right'caption='[[1l76]], [[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'>[[1l76]] 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=1L76 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1L76 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=1l76 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1l76 OCA], [https://pdbe.org/1l76 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1l76 RCSB], [https://www.ebi.ac.uk/pdbsum/1l76 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1l76 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/l7/1l76_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=1l76 ConSurf].
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<div style="clear:both"></div>
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'''TOLERANCE OF T4 LYSOZYME TO PROLINE SUBSTITUTIONS WITHIN THE LONG INTERDOMAIN ALPHA-HELIX ILLUSTRATES THE ADAPTABILITY OF PROTEINS TO POTENTIALLY DESTABILIZING LESIONS'''
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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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To investigate the ability of a protein to accommodate potentially destabilizing amino acid substitutions, and also to investigate the steric requirements for catalysis, proline was substituted at different sites within the long alpha-helix that connects the amino-terminal and carboxyl-terminal domains of T4 lysozyme. Of the four substitutions attempted, three yielded folded, functional proteins. The catalytic activities of these three mutant proteins (Q69P, D72P, and A74P) were 60-90% that of wild-type. Their melting temperatures were 7-12 degrees C less than that of wild-type at pH 6.5. Mutant D72P formed crystals isomorphous with wild-type allowing the structure to be determined at high resolution. In the crystal structure of wild-type lysozyme the interdomain alpha-helix has an overall bend angle of 8.5 degrees. In the mutant structure the introduction of the proline causes this bend angle to increase to 14 degrees and also causes a corresponding rotation of 5.5 degrees of carboxyl-terminal domain relative to the amino-terminal one. Except for the immediate location of the proline substitution there is very little change in the geometry of the interdomain alpha-helix. The results support the view that protein structures are adaptable and can compensate for potentially destabilizing amino acid substitutions. The results also suggest that the precise shape of the active site cleft of T4 lysozyme is not critical for catalysis.
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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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1L76 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacteriophage_t4 Bacteriophage t4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1L76 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: Sauer U]]
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Tolerance of T4 lysozyme to proline substitutions within the long interdomain alpha-helix illustrates the adaptability of proteins to potentially destabilizing lesions., Sauer UH, San DP, Matthews BW, J Biol Chem. 1992 Feb 5;267(4):2393-9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/1733941 1733941]
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[[Category: Bacteriophage t4]]
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[[Category: Lysozyme]]
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[[Category: Single protein]]
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[[Category: Matthews, B W.]]
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[[Category: Sauer, U.]]
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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

TOLERANCE OF T4 LYSOZYME TO PROLINE SUBSTITUTIONS WITHIN THE LONG INTERDOMAIN ALPHA-HELIX ILLUSTRATES THE ADAPTABILITY OF PROTEINS TO POTENTIALLY DESTABILIZING LESIONS

PDB ID 1l76

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