View source for 2kac


==NMR solution structure of KX6E protL mutant==
<StructureSection load='2kac' size='340' side='right'caption='[[2kac]]' scene=''>
== Structural highlights ==
<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>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
<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>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q51912_FINMA Q51912_FINMA] 
== 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/ka/2kac_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=2kac ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.

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>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2kac" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Finegoldia magna]]
[[Category: Large Structures]]
[[Category: Lopez-Mendez B]]
[[Category: Millet O]]
[[Category: Pons M]]
[[Category: Tadeo X]]