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1kfm

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{{Seed}}
 
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[[Image:1kfm.png|left|200px]]
 
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==Core side-chain packing and backbone conformation in Lpp-56 coiled-coil mutants==
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The line below this paragraph, containing "STRUCTURE_1kfm", creates the "Structure Box" on the page.
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<StructureSection load='1kfm' size='340' side='right'caption='[[1kfm]], [[Resolution|resolution]] 2.00&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'>[[1kfm]] 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=1KFM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KFM 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&#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=1kfm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kfm OCA], [https://pdbe.org/1kfm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1kfm RCSB], [https://www.ebi.ac.uk/pdbsum/1kfm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1kfm ProSAT]</span></td></tr>
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{{STRUCTURE_1kfm| PDB=1kfm | SCENE= }}
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</table>
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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/1kfm_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=1kfm 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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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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===Core side-chain packing and backbone conformation in Lpp-56 coiled-coil mutants===
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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:12054830<ref>PMID:12054830</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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The line below this paragraph, {{ABSTRACT_PUBMED_12054830}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 1kfm" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 12054830 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_12054830}}
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__TOC__
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</StructureSection>
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==About this Structure==
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1KFM is a 1 chain 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=1KFM OCA].
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==Reference==
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<ref group="xtra">PMID:12054830</ref><references group="xtra"/>
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Cao, W.]]
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[[Category: Large Structures]]
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[[Category: Liu, J.]]
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[[Category: Cao W]]
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[[Category: Lu, M.]]
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[[Category: Liu J]]
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[[Category: Alanine-zipper]]
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[[Category: Lu M]]
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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://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 23:58:35 2009''
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Current revision

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

PDB ID 1kfm

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