1oyu

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{{Seed}}
 
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[[Image:1oyu.png|left|200px]]
 
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==Long-Distance conformational changes in a protein engineered by modulated sequence duplication==
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The line below this paragraph, containing "STRUCTURE_1oyu", creates the "Structure Box" on the page.
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<StructureSection load='1oyu' size='340' side='right'caption='[[1oyu]], [[Resolution|resolution]] 2.50&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'>[[1oyu]] 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=1OYU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OYU 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]] 2.5&#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=1oyu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1oyu OCA], [https://pdbe.org/1oyu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1oyu RCSB], [https://www.ebi.ac.uk/pdbsum/1oyu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1oyu ProSAT]</span></td></tr>
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{{STRUCTURE_1oyu| PDB=1oyu | 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/oy/1oyu_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=1oyu 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 ==
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There are few, if any, known instances in which a biological signal is transmitted via a large conformational change through the body of a protein. We describe here a mutant of T4 lysozyme that was engineered to permit structural change at a distance. The design uses a tandem sequence repeat that makes it possible to transmit large-scale structural changes from one end of an alpha-helix to the other over a distance of 17-25 A. The method should be of general applicability and may make it possible to introduce a mutation at one site in a protein that will induce large-scale changes in the structure at a spatially remote site.
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===Long-Distance conformational changes in a protein engineered by modulated sequence duplication===
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Long-distance conformational changes in a protein engineered by modulated sequence duplication.,Sagermann M, Gay L, Matthews BW Proc Natl Acad Sci U S A. 2003 Aug 5;100(16):9191-5. Epub 2003 Jul 17. PMID:12869697<ref>PMID:12869697</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1oyu" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_12869697}}, adds the Publication Abstract to the page
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*[[Lysozyme 3D structures|Lysozyme 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 12869697 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_12869697}}
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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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1OYU is a 2 chains structure of sequences 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=1OYU OCA].
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[[Category: Large Structures]]
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[[Category: Gay L]]
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==Reference==
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[[Category: Matthews BW]]
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<ref group="xtra">PMID:12869697</ref><references group="xtra"/>
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[[Category: Sagermann M]]
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[[Category: Enterobacteria phage t4]]
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[[Category: Lysozyme]]
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[[Category: Gay, L.]]
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[[Category: Matthews, B W.]]
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[[Category: Sagermann, M.]]
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[[Category: Design of structural switch]]
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[[Category: Protein design]]
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[[Category: Sequence duplication]]
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[[Category: Tandem repeat]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 14:06:39 2009''
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Current revision

Long-Distance conformational changes in a protein engineered by modulated sequence duplication

PDB ID 1oyu

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