1kfm: Difference between revisions

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{{Seed}}
[[Image:1kfm.png|left|200px]]


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==Core side-chain packing and backbone conformation in Lpp-56 coiled-coil mutants==
The line below this paragraph, containing "STRUCTURE_1kfm", creates the "Structure Box" on the page.
<StructureSection load='1kfm' size='340' side='right'caption='[[1kfm]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)  
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<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>
or leave the SCENE parameter empty for the default display.
</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>
{{STRUCTURE_1kfm|  PDB=1kfm  |  SCENE=  }}
</table>
== Function ==
[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.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/kf/1kfm_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.


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


 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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The line below this paragraph, {{ABSTRACT_PUBMED_12054830}}, adds the Publication Abstract to the page
<div class="pdbe-citations 1kfm" style="background-color:#fffaf0;"></div>
(as it appears on PubMed at http://www.pubmed.gov), where 12054830 is the PubMed ID number.
== References ==
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<references/>
{{ABSTRACT_PUBMED_12054830}}
__TOC__
 
</StructureSection>
==About this Structure==
1KFM 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=1KFM OCA].
 
==Reference==
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://www.ncbi.nlm.nih.gov/pubmed/12054830 12054830]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Cao, W.]]
[[Category: Cao W]]
[[Category: Liu, J.]]
[[Category: Liu J]]
[[Category: Lu, M.]]
[[Category: Lu M]]
[[Category: Alanine-zipper]]
[[Category: Coiled coil]]
[[Category: Helix capping]]
[[Category: Lipoprotein]]
[[Category: Protein folding]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul  2 10:16:10 2008''
Retrieved from "https://proteopedia.org/1kfm"