2vnl

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{{Seed}}
 
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[[Image:2vnl.jpg|left|200px]]
 
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==MUTANT Y108Wdel OF THE HEADBINDING DOMAIN OF PHAGE P22 TAILSPIKE C- TERMINally fused to ISOLEUCINE ZIPPER pIIGCN4 (chimera II)==
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The line below this paragraph, containing "STRUCTURE_2vnl", creates the "Structure Box" on the page.
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<StructureSection load='2vnl' size='340' side='right'caption='[[2vnl]], [[Resolution|resolution]] 1.80&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'>[[2vnl]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] and [https://en.wikipedia.org/wiki/Salmonella_virus_P22 Salmonella virus P22]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VNL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VNL 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]] 1.8&#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=GOL:GLYCEROL'>GOL</scene></td></tr>
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{{STRUCTURE_2vnl| PDB=2vnl | SCENE= }}
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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=2vnl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vnl OCA], [https://pdbe.org/2vnl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vnl RCSB], [https://www.ebi.ac.uk/pdbsum/2vnl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vnl ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/GCN4_YEAST GCN4_YEAST] Is a transcription factor that is responsible for the activation of more than 30 genes required for amino acid or for purine biosynthesis in response to amino acid or purine starvation. Binds and recognize the DNA sequence: 5'-TGA[CG]TCA-3'.[https://www.uniprot.org/uniprot/FIBER_BPP22 FIBER_BPP22] Structural component of the short non-contractile tail. The tail comprises six fibers that mediate primary attachment to the host cell lipopolysaccharides (LPS) and display endorhamnosidase enzymatic activity, hydrolyzing the alpha-1,3-O-glycosidic linkage between rhamnose and galactose of the O-antigen polysaccharide. Digestion of the LPS brings the capsid near the cell outer membrane.<ref>PMID:12837775</ref> <ref>PMID:20817910</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/vn/2vnl_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=2vnl 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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Attachment of phages to host cells, followed by phage DNA ejection, represents the first stage of viral infection of bacteria. Salmonella phage P22 has been extensively studied, serving as an experimental model for bacterial infection by phages. P22 engages bacteria by binding to the sugar moiety of lipopolysaccharides using the viral tailspike protein for attachment. While the structures of the N-terminal particle-binding domain and the major receptor-binding domain of the tailspike have been analyzed individually, the three-dimensional organization of the intact protein, including the highly conserved linker region between the two domains, remained unknown. A single amino-acid exchange in the linker sequence made it possible to crystallize the full-length protein. Two crystal structures of the linker region are presented: one attached to the N-terminal domain and the other present within the complete tailspike protein. Both retain their biological function, but the mutated full-length tailspike displays a retarded folding pathway. Fitting of the full-length tailspike into a published cryo-electron microscopy map of the P22 virion requires an elastic distortion of the crystal structure. The conservation of the linker suggests a role in signal transmission from the distal tip of the molecule to the phage head, eventually leading to DNA ejection.
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===MUTANT Y108WDEL OF THE HEADBINDING DOMAIN OF PHAGE P22 TAILSPIKE C-TERMINALLY FUSED TO ISOLEUCINE ZIPPER PIIGCN4 (CHIMERA II)===
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Bacteriophage P22 tailspike: structure of the complete protein and function of the interdomain linker.,Seul A, Muller JJ, Andres D, Stettner E, Heinemann U, Seckler R Acta Crystallogr D Biol Crystallogr. 2014 May;70(Pt 5):1336-45. doi:, 10.1107/S1399004714002685. Epub 2014 Apr 30. PMID:24816102<ref>PMID:24816102</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 2vnl" style="background-color:#fffaf0;"></div>
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==About this Structure==
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==See Also==
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2VNL is a 2 chains structure of sequences from [http://en.wikipedia.org/wiki/Enterobacteria_phage_p22,_saccharomyces_cerevisiae Enterobacteria phage p22, saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VNL OCA].
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*[[Tailspike protein 3D structures|Tailspike protein 3D structures]]
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[[Category: Enterobacteria phage p22, saccharomyces cerevisiae]]
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== References ==
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[[Category: Heinemann, U.]]
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<references/>
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[[Category: Mueller, G.]]
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__TOC__
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[[Category: Mueller, J J.]]
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</StructureSection>
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[[Category: Seckler, R.]]
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[[Category: Large Structures]]
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[[Category: Seul, A.]]
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[[Category: Saccharomyces cerevisiae]]
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[[Category: Chimera]]
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[[Category: Salmonella virus P22]]
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[[Category: Head-binding domain]]
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[[Category: Heinemann U]]
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[[Category: Hydrolase]]
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[[Category: Mueller G]]
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[[Category: Isoleucine zipper piigcn4]]
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[[Category: Mueller JJ]]
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[[Category: Late protein]]
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[[Category: Seckler R]]
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[[Category: Mutant y108wdel]]
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[[Category: Seul A]]
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[[Category: Phage p22 tailspike protein]]
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[[Category: Viral protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 11 14:24:14 2009''
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Current revision

MUTANT Y108Wdel OF THE HEADBINDING DOMAIN OF PHAGE P22 TAILSPIKE C- TERMINally fused to ISOLEUCINE ZIPPER pIIGCN4 (chimera II)

PDB ID 2vnl

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