1l34

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[[Image:1l34.jpg|left|200px]]
 
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{{Structure
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==HIGH-RESOLUTION STRUCTURE OF THE TEMPERATURE-SENSITIVE MUTANT OF PHAGE LYSOZYME, ARG 96 (RIGHT ARROW) HIS==
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|PDB= 1l34 |SIZE=350|CAPTION= <scene name='initialview01'>1l34</scene>, resolution 1.9&Aring;
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<StructureSection load='1l34' size='340' side='right'caption='[[1l34]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND=
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<table><tr><td colspan='2'>[[1l34]] 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=1L34 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1L34 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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1l34 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1l34 OCA], [https://pdbe.org/1l34 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1l34 RCSB], [https://www.ebi.ac.uk/pdbsum/1l34 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1l34 ProSAT]</span></td></tr>
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}}
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</table>
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== Function ==
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'''HIGH-RESOLUTION STRUCTURE OF THE TEMPERATURE-SENSITIVE MUTANT OF PHAGE LYSOZYME, ARG 96 (RIGHT ARROW) HIS'''
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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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==Overview==
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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/l3/1l34_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=1l34 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 ==
The structure of the temperature-sensitive mutant lysozyme of bacteriophage T4 in which arginine 96 is replaced by histidine has been determined crystallographically and refined to a residual of 17.6% at 1.9-A resolution. Overall, the three-dimensional structure of the mutant protein is extremely similar to that of wild type. There are local distortions in the mutant structure suggesting that the substituted His 96 residue is under strain. This appears to be one of the major reasons for the decreased thermostability. In wild-type lysozyme the guanidinium of Arg 96 is located at the carboxy terminus of alpha-helix 82-90 and makes a pair of hydrogen bonds to two of the carbonyl groups in the last turn of the helix. The loss of this "helix dipole" interaction also appears to contribute to the destabilization. The pKa* of His 96 in the mutant lysozyme has been determined by nuclear magnetic resonance and found to be 6.8 at 10 degrees C. This relatively normal value of the histidine pKa* suggests that the protonated and unprotonated forms of the imidazole ring are perturbed equally by the protein environment or, what is equivalent, the mutant lysozyme is equally stable with either histidine species.
The structure of the temperature-sensitive mutant lysozyme of bacteriophage T4 in which arginine 96 is replaced by histidine has been determined crystallographically and refined to a residual of 17.6% at 1.9-A resolution. Overall, the three-dimensional structure of the mutant protein is extremely similar to that of wild type. There are local distortions in the mutant structure suggesting that the substituted His 96 residue is under strain. This appears to be one of the major reasons for the decreased thermostability. In wild-type lysozyme the guanidinium of Arg 96 is located at the carboxy terminus of alpha-helix 82-90 and makes a pair of hydrogen bonds to two of the carbonyl groups in the last turn of the helix. The loss of this "helix dipole" interaction also appears to contribute to the destabilization. The pKa* of His 96 in the mutant lysozyme has been determined by nuclear magnetic resonance and found to be 6.8 at 10 degrees C. This relatively normal value of the histidine pKa* suggests that the protonated and unprotonated forms of the imidazole ring are perturbed equally by the protein environment or, what is equivalent, the mutant lysozyme is equally stable with either histidine species.
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==About this Structure==
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High-resolution structure of the temperature-sensitive mutant of phage lysozyme, Arg 96----His.,Weaver LH, Gray TM, Grutter MG, Anderson DE, Wozniak JA, Dahlquist FW, Matthews BW Biochemistry. 1989 May 2;28(9):3793-7. PMID:2665808<ref>PMID:2665808</ref>
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1L34 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=1L34 OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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High-resolution structure of the temperature-sensitive mutant of phage lysozyme, Arg 96----His., Weaver LH, Gray TM, Grutter MG, Anderson DE, Wozniak JA, Dahlquist FW, Matthews BW, Biochemistry. 1989 May 2;28(9):3793-7. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/2665808 2665808]
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</div>
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[[Category: Bacteriophage t4]]
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<div class="pdbe-citations 1l34" style="background-color:#fffaf0;"></div>
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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: Weaver, L H.]]
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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 12:25:40 2008''
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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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<references/>
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__TOC__
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</StructureSection>
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[[Category: Escherichia virus T4]]
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[[Category: Large Structures]]
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[[Category: Matthews BW]]
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[[Category: Weaver LH]]

Current revision

HIGH-RESOLUTION STRUCTURE OF THE TEMPERATURE-SENSITIVE MUTANT OF PHAGE LYSOZYME, ARG 96 (RIGHT ARROW) HIS

PDB ID 1l34

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