1kfn

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(New page: 200px<br /><applet load="1kfn" size="450" color="white" frame="true" align="right" spinBox="true" caption="1kfn, resolution 1.65&Aring;" /> '''Core side-chain pack...)
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[[Image:1kfn.gif|left|200px]]<br /><applet load="1kfn" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1kfn, resolution 1.65&Aring;" />
 
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'''Core side-chain packing and backbone conformation in Lpp-56 coiled-coil mutants'''<br />
 
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==Overview==
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==Core side-chain packing and backbone conformation in Lpp-56 coiled-coil mutants==
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Native proteins exhibit precise geometric packing of atoms in their, hydrophobic interiors. Nonetheless, controversy remains about the role of, core side-chain packing in specifying and stabilizing the folded, structures of proteins. Here we investigate the role of core packing in, determining the conformation and stability of the Lpp-56 trimerization, domain. The X-ray crystal structures of Lpp-56 mutants with alanine, substitutions at two and four interior core positions reveal trimeric, coiled coils in which the twist of individual helices and the helix-helix, spacing vary significantly to achieve the most favored superhelical, packing arrangement. Introduction of each alanine "layer" into the, hydrophobic core destabilizes the superhelix by 1.4 kcal mol(-1). Although, the methyl groups of the alanine residues pack at their optimum van der, Waals contacts in the coiled-coil trimer, they provide a smaller component, of hydrophobic interactions than bulky hydrophobic side-chains to the, thermodynamic stability. Thus, specific side-chain packing in the, hydrophobic core of coiled coils are important determinants of protein, main-chain conformation and stability.
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<StructureSection load='1kfn' size='340' side='right'caption='[[1kfn]], [[Resolution|resolution]] 1.65&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[1kfn]] 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=1KFN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KFN FirstGlance]. <br>
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1KFN 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=1KFN 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]] 1.65&#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=1kfn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kfn OCA], [https://pdbe.org/1kfn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1kfn RCSB], [https://www.ebi.ac.uk/pdbsum/1kfn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1kfn ProSAT]</span></td></tr>
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==Reference==
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</table>
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Core side-chain packing and backbone conformation in Lpp-56 coiled-coil mutants., Liu J, Cao W, Lu M, J Mol Biol. 2002 May 3;318(3):877-88. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12054830 12054830]
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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/kf/1kfn_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=1kfn 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: Cao, W.]]
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[[Category: Cao W]]
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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: alanine-zipper]]
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[[Category: coiled coil]]
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[[Category: helix capping]]
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[[Category: lipoprotein]]
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[[Category: protein folding]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 19:10:20 2007''
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Current revision

Core side-chain packing and backbone conformation in Lpp-56 coiled-coil mutants

PDB ID 1kfn

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