2gus

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[[Image:2gus.gif|left|200px]]
 
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==Conformational Transition between Four- and Five-stranded Phenylalanine Zippers Determined by a Local Packing Interaction==
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The line below this paragraph, containing "STRUCTURE_2gus", creates the "Structure Box" on the page.
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<StructureSection load='2gus' size='340' side='right'caption='[[2gus]], [[Resolution|resolution]] 1.75&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'>[[2gus]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GUS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2GUS 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]] 1.75&#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=2gus FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gus OCA], [https://pdbe.org/2gus PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2gus RCSB], [https://www.ebi.ac.uk/pdbsum/2gus PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2gus ProSAT]</span></td></tr>
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{{STRUCTURE_2gus| PDB=2gus | SCENE= }}
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</table>
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== Function ==
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'''Conformational Transition between Four- and Five-stranded Phenylalanine Zippers Determined by a Local Packing Interaction'''
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[https://www.uniprot.org/uniprot/LPP_ECOLI LPP_ECOLI] Interacts with the peptidoglycan both covalently and noncovalently. This interaction contributes to the maintenance of the structural and functional integrity of the cell envelope.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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==Overview==
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Check<jmol>
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Alpha-helical coiled coils play a crucial role in mediating specific protein-protein interactions. However, the rules and mechanisms that govern helix-helix association in coiled coils remain incompletely understood. Here we have engineered a seven heptad "Phe-zipper" protein (Phe-14) with phenylalanine residues at all 14 hydrophobic a and d positions, and generated a further variant (Phe-14(M)) in which a single core Phe residue is substituted with Met. Phe-14 forms a discrete alpha-helical pentamer in aqueous solution, while Phe-14(M) folds into a tetrameric helical structure. X-ray crystal structures reveal that in both the tetramer and the pentamer the a and d side-chains interlock in a classical knobs-into-holes packing to produce parallel coiled-coil structures enclosing large tubular cavities. However, the presence of the Met residue in the apolar interface of the tetramer markedly alters its local coiled-coil conformation and superhelical geometry. Thus, short-range interactions involving the Met side-chain serve to preferentially select for tetramer formation, either by inhibiting a nucleation step essential for pentamer folding or by abrogating an intermediate required to form the pentamer. Although specific trigger sequences have not been clearly identified in dimeric coiled coils, higher-order coiled coils, as well as other oligomeric multi-protein complexes, may require such sequences to nucleate and direct their assembly.
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gu/2gus_consurf.spt"</scriptWhenChecked>
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==About this Structure==
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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2GUS is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GUS OCA].
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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==Reference==
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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=2gus ConSurf].
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Conformational transition between four and five-stranded phenylalanine zippers determined by a local packing interaction., Liu J, Zheng Q, Deng Y, Kallenbach NR, Lu M, J Mol Biol. 2006 Aug 4;361(1):168-79. Epub 2006 Jun 13. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16828114 16828114]
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<div style="clear:both"></div>
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__TOC__
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</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Deng, Y.]]
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[[Category: Deng Y]]
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[[Category: Kallenbach, N R.]]
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[[Category: Kallenbach NR]]
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[[Category: Liu, J.]]
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[[Category: Liu J]]
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[[Category: Lu, M.]]
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[[Category: Lu M]]
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[[Category: Zheng, Q.]]
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[[Category: Zheng Q]]
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[[Category: Coiled coil]]
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[[Category: Lipoprotein]]
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[[Category: Phenylalanine-zipper]]
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[[Category: Protein folding]]
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[[Category: Tetramer]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 05:33:46 2008''
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Current revision

Conformational Transition between Four- and Five-stranded Phenylalanine Zippers Determined by a Local Packing Interaction

PDB ID 2gus

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