142l

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(New page: 200px<br /><applet load="142l" size="450" color="white" frame="true" align="right" spinBox="true" caption="142l, resolution 2.00&Aring;" /> '''ROLE OF BACKBONE FLE...)
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[[Image:142l.jpg|left|200px]]<br /><applet load="142l" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="142l, resolution 2.00&Aring;" />
 
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'''ROLE OF BACKBONE FLEXIBILITY IN THE ACCOMMODATION OF VARIANTS THAT REPACK THE CORE OF T4 LYSOZYME'''<br />
 
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==Overview==
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==ROLE OF BACKBONE FLEXIBILITY IN THE ACCOMMODATION OF VARIANTS THAT REPACK THE CORE OF T4 LYSOZYME==
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To understand better how the packing of side chains within the core, influences protein structure and stability, the crystal structures were, determined for eight variants of T4 lysozyme, each of which contains three, to five substitutions at adjacent interior sites. Concerted main-chain and, side-chain displacements, with movements of helical segments as large as, 0.8 angstrom, were observed. In contrast, the angular conformations of the, mutated side chains tended to remain unchanged, with torsion angles within, 20 degrees of those in the wild-type structure. These observations suggest, that not only the rotation of side chains but also movements of the main, chain must be considered in the evaluation of which amino acid sequences, are compatible with a given protein fold.
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<StructureSection load='142l' size='340' side='right'caption='[[142l]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[142l]] 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=142L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=142L 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&#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=142l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=142l OCA], [https://pdbe.org/142l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=142l RCSB], [https://www.ebi.ac.uk/pdbsum/142l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=142l 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/42/142l_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=142l 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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142L 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=142L 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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The role of backbone flexibility in the accommodation of variants that repack the core of T4 lysozyme., Baldwin EP, Hajiseyedjavadi O, Baase WA, Matthews BW, Science. 1993 Dec 10;262(5140):1715-8. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8259514 8259514]
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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: Baldwin, E.]]
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[[Category: Baldwin E]]
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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 10:27:14 2007''
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Current revision

ROLE OF BACKBONE FLEXIBILITY IN THE ACCOMMODATION OF VARIANTS THAT REPACK THE CORE OF T4 LYSOZYME

PDB ID 142l

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