1t97

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[[Image:1t97.jpg|left|200px]]
 
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==Use of sequence duplication to engineer a ligand-triggered long-distance molecular switch in T4 Lysozyme==
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The line below this paragraph, containing "STRUCTURE_1t97", creates the "Structure Box" on the page.
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<StructureSection load='1t97' size='340' side='right'caption='[[1t97]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1t97]] is a 2 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=1T97 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1T97 FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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]] 2.7&#8491;</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=1t97 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1t97 OCA], [https://pdbe.org/1t97 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1t97 RCSB], [https://www.ebi.ac.uk/pdbsum/1t97 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1t97 ProSAT]</span></td></tr>
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{{STRUCTURE_1t97| PDB=1t97 | SCENE= }}
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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/t9/1t97_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=1t97 ConSurf].
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<div style="clear:both"></div>
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'''Use of sequence duplication to engineer a ligand-triggered long-distance molecular switch in T4 lysosyme'''
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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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We have designed a molecular switch in a T4 lysozyme construct that controls a large-scale translation of a duplicated helix. As shown by crystal structures of the construct with the switch on and off, the conformational change is triggered by the binding of a ligand (guanidinium ion) to a site that in the wild-type protein was occupied by the guanidino head group of an Arg. In the design template, a duplicated helix is flanked by two loop regions of different stabilities. In the "on" state, the N-terminal loop is weakly structured, whereas the C-terminal loop has a well defined conformation that is stabilized by means of nonbonded interactions with the Arg head group. The truncation of the Arg to Ala destabilizes this loop and switches the protein to the "off" state, in which the duplicated helix is translocated approximately 20 A. Guanidinium binding restores the key interactions, restabilizes the C-terminal loop, and restores the "on" state. Thus, the presence of an external ligand, which is unrelated to the catalytic activity of the enzyme, triggers the inserted helix to translate 20 A away from the binding site. The results illustrate a proposed mechanism for protein evolution in which sequence duplication followed by point mutation can lead to the establishment of new function.
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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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1T97 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Enterobacteria_phage_t4 Enterobacteria phage t4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1T97 OCA].
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[[Category: Large Structures]]
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[[Category: Baase WA]]
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==Reference==
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[[Category: Matthews BW]]
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Use of sequence duplication to engineer a ligand-triggered, long-distance molecular switch in T4 lysozyme., Yousef MS, Baase WA, Matthews BW, Proc Natl Acad Sci U S A. 2004 Aug 10;101(32):11583-6. Epub 2004 Jul 30. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15286283 15286283]
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[[Category: Yousef MS]]
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[[Category: Enterobacteria phage t4]]
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[[Category: Lysozyme]]
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[[Category: Single protein]]
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[[Category: Baase, W A.]]
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[[Category: Matthews, B W.]]
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[[Category: Yousef, M S.]]
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[[Category: Molecular switch]]
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[[Category: Nano-biotechnology]]
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[[Category: Protein design]]
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[[Category: Protein engineering]]
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[[Category: Sequence duplication]]
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[[Category: T4 lysozyme]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 09:41:43 2008''
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Current revision

Use of sequence duplication to engineer a ligand-triggered long-distance molecular switch in T4 Lysozyme

PDB ID 1t97

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