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1cu3

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(New page: 200px<br /><applet load="1cu3" size="450" color="white" frame="true" align="right" spinBox="true" caption="1cu3, resolution 2.12&Aring;" /> '''T4 LYSOZYME MUTANT V...)
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[[Image:1cu3.gif|left|200px]]<br /><applet load="1cu3" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1cu3, resolution 2.12&Aring;" />
 
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'''T4 LYSOZYME MUTANT V87M'''<br />
 
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==Overview==
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==T4 LYSOZYME MUTANT V87M==
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In an attempt to identify a systematic relation between the structure of a, protein and its folding kinetics, the rate of folding was determined for, 20 mutants of T4 lysozyme in which a bulky, buried, nonpolar wild-type, residue (Leu, Ile, Phe, Val, or Met) was substituted with alanine., Methionine, which approximated the size of the original side chain but, which is of different shape and flexibility, was also substituted at most, of the same sites. Mutations that substantially destabilize the protein, and are located in the carboxy-terminal domain generally slow the rate of, folding. Destabilizing mutations in the amino-terminal domain, however, have little effect on the rate of folding. Mutations that have little, effect on stability tend to have little effect on the rate, no matter, where they are located. These results suggest that, at the rate-limiting, step, elements of structure in the C-terminal domain are formed and have a, structure similar to that of the fully folded protein. Consistent with, this, two variants that somewhat increase the rate of folding (Phe104 --&gt;, Met and Val149 --&gt; Met) are located within the carboxy-terminal domain and, maintain or improve packing with very little perturbation of the wild-type, structure.
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<StructureSection load='1cu3' size='340' side='right'caption='[[1cu3]], [[Resolution|resolution]] 2.12&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1cu3]] 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=1CU3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CU3 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]] 2.12&#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=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=HED:2-HYDROXYETHYL+DISULFIDE'>HED</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=1cu3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cu3 OCA], [https://pdbe.org/1cu3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1cu3 RCSB], [https://www.ebi.ac.uk/pdbsum/1cu3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cu3 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/cu/1cu3_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=1cu3 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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1CU3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacteriophage_t4 Bacteriophage t4] with CL and HED 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=1CU3 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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Methionine and alanine substitutions show that the formation of wild-type-like structure in the carboxy-terminal domain of T4 lysozyme is a rate-limiting step in folding., Gassner NC, Baase WA, Lindstrom JD, Lu J, Dahlquist FW, Matthews BW, Biochemistry. 1999 Nov 2;38(44):14451-60. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10545167 10545167]
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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: Baase, W.A.]]
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[[Category: Baase WA]]
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[[Category: Gassner, N.C.]]
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[[Category: Gassner NC]]
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[[Category: Lindstrom, J.D.]]
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[[Category: Lindstrom JD]]
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[[Category: Lu, J.]]
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[[Category: Lu J]]
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[[Category: Matthews, B.W.]]
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[[Category: Matthews BW]]
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[[Category: CL]]
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[[Category: HED]]
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[[Category: hydrolase (o-glycosyl)]]
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[[Category: methionine core mutant]]
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[[Category: protein engineering]]
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[[Category: protein folding]]
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[[Category: t4 lysozyme]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 12:45:51 2007''
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Current revision

T4 LYSOZYME MUTANT V87M

PDB ID 1cu3

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