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139l

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(New page: 200px<br /><applet load="139l" size="450" color="white" frame="true" align="right" spinBox="true" caption="139l, resolution 1.7&Aring;" /> '''RAPID CRYSTALLIZATION...)
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[[Image:139l.jpg|left|200px]]<br /><applet load="139l" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="139l, resolution 1.7&Aring;" />
 
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'''RAPID CRYSTALLIZATION OF T4 LYSOZYME BY INTERMOLECULAR DISULFIDE CROSSLINKING'''<br />
 
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==Overview==
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==RAPID CRYSTALLIZATION OF T4 LYSOZYME BY INTERMOLECULAR DISULFIDE CROSSLINKING==
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In an attempt to facilitate crystallization, engineered cysteines were, used to promote formation of a 'back-to-back' dimer that occurs in, different crystal forms of wild-type and mutant T4 lysozymes. The designed, double mutant, N68C/A93C, in which the surface residues Asn68 and Ala93, were replaced by cysteines, formed dimers in solution and crystallized, isomorphously to wild-type, but at a much faster rate. Overall, the mutant, structure remained very similar to wild-type despite the formation of two, intermolecular disulfide bridges. The crystals of cross-linked dimers ahd, thermal factors somewhat lower than wild-type, indicating reduced, mobility, but did not diffract to noticeably higher resolution., Introduction of the same cross-links was also used to obtain crystals in a, different space group of a T4 lysozyme mutant that could not be, crystallized previously. The results suggest that the formation of the, lysozyme dimer is a critical intermediate in the formation of more than, one crystal form and that covalent cross-linking of the intermediate, accelerates nucleation and facilitates crystal growth. The disulfide, cross-links are located on the 'back' of the molecule and formation of the, cross-linked dimer appears to leave the active sites completely, unobstructed. Nevertheless, the cross-linked dimer is completely inactive., One explanation for this behavior is that the disulfide bridges prevent, hinge-bending motion that may be required for catalysis. Another, possibility is that the formation of the dimer increases the overall bulk, of the enzyme and prevents its access to the susceptible glycosidic bonds, within the cell wall substrate.
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<StructureSection load='139l' size='340' side='right'caption='[[139l]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[139l]] 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=139L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=139L 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='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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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=139l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=139l OCA], [https://pdbe.org/139l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=139l RCSB], [https://www.ebi.ac.uk/pdbsum/139l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=139l 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/39/139l_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=139l 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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139L is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Enterobacteria_phage_t2 Enterobacteria phage t2] with CL and BME as [http://en.wikipedia.org/wiki/ligands ligands]. 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=139L 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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Rapid crystallization of T4 lysozyme by intermolecular disulfide cross-linking., Heinz DW, Matthews BW, Protein Eng. 1994 Mar;7(3):301-7. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8177878 8177878]
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__TOC__
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[[Category: Enterobacteria phage t2]]
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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: Heinz, D.W.]]
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[[Category: Heinz DW]]
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[[Category: Matthews, B.W.]]
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[[Category: Matthews BW]]
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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://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 10:26:57 2007''
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Current revision

RAPID CRYSTALLIZATION OF T4 LYSOZYME BY INTERMOLECULAR DISULFIDE CROSSLINKING

PDB ID 139l

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