2kac

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[[Image:2kac.png|left|200px]]
 
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==NMR solution structure of KX6E protL mutant==
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The line below this paragraph, containing "STRUCTURE_2kac", creates the "Structure Box" on the page.
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<StructureSection load='2kac' size='340' side='right'caption='[[2kac]]' 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'>[[2kac]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Finegoldia_magna Finegoldia magna]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KAC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2KAC 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">Solution NMR</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=2kac FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2kac OCA], [https://pdbe.org/2kac PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2kac RCSB], [https://www.ebi.ac.uk/pdbsum/2kac PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2kac ProSAT]</span></td></tr>
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{{STRUCTURE_2kac| PDB=2kac | SCENE= }}
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/Q51912_FINMA Q51912_FINMA]
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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/ka/2kac_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=2kac 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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Proteins from halophilic organisms, which live in extreme saline conditions, have evolved to remain folded at very high ionic strengths. The surfaces of halophilic proteins show a biased amino acid composition with a high prevalence of aspartic and glutamic acids, a low frequency of lysine, and a high occurrence of amino acids with a low hydrophobic character. Using extensive mutational studies on the protein surfaces, we show that it is possible to decrease the salt dependence of a typical halophilic protein to the level of a mesophilic form and engineer a protein from a mesophilic organism into an obligate halophilic form. NMR studies demonstrate complete preservation of the three-dimensional structure of extreme mutants and confirm that salt dependency is conferred exclusively by surface residues. In spite of the statistically established fact that most halophilic proteins are strongly acidic, analysis of a very large number of mutants showed that the effect of salt on protein stability is largely independent of the total protein charge. Conversely, we quantitatively demonstrate that halophilicity is directly related to a decrease in the accessible surface area.
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===NMR solution structure of KX6E protL mutant===
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Structural basis for the aminoacid composition of proteins from halophilic archea.,Tadeo X, Lopez-Mendez B, Trigueros T, Lain A, Castano D, Millet O PLoS Biol. 2009 Dec;7(12):e1000257. Epub 2009 Dec 15. PMID:20016684<ref>PMID:20016684</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_20016684}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 2kac" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 20016684 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_20016684}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[2kac]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Finegoldia_magna Finegoldia magna]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KAC OCA].
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==Reference==
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<ref group="xtra">PMID:20016684</ref><ref group="xtra">PMID:19883603</ref><references group="xtra"/>
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[[Category: Finegoldia magna]]
[[Category: Finegoldia magna]]
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[[Category: Lopez-Mendez, B.]]
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[[Category: Large Structures]]
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[[Category: Millet, O.]]
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[[Category: Lopez-Mendez B]]
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[[Category: Pons, M.]]
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[[Category: Millet O]]
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[[Category: Tadeo, X.]]
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[[Category: Pons M]]
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[[Category: Cell wall]]
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[[Category: Tadeo X]]
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[[Category: Immune system]]
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[[Category: Peptidoglycan-anchor]]
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[[Category: Protein]]
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Current revision

NMR solution structure of KX6E protL mutant

PDB ID 2kac

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