2gus

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(New page: 200px<br /><applet load="2gus" size="450" color="white" frame="true" align="right" spinBox="true" caption="2gus, resolution 1.75&Aring;" /> '''Conformational Trans...)
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[[Image:2gus.gif|left|200px]]<br /><applet load="2gus" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="2gus, resolution 1.75&Aring;" />
 
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'''Conformational Transition between Four- and Five-stranded Phenylalanine Zippers Determined by a Local Packing Interaction'''<br />
 
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==Overview==
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==Conformational Transition between Four- and Five-stranded Phenylalanine Zippers Determined by a Local Packing Interaction==
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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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<StructureSection load='2gus' size='340' side='right'caption='[[2gus]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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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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2GUS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2GUS OCA].
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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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==Reference==
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</table>
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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://ispc.weizmann.ac.il//pmbin/getpm?pmid=16828114 16828114]
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== Function ==
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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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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/gu/2gus_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=2gus ConSurf].
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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://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 11:24:06 2007''
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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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