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| | ==NMR solution structure of KX6E protL mutant== | | ==NMR solution structure of KX6E protL mutant== |
| - | <StructureSection load='2kac' size='340' side='right'caption='[[2kac]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='2kac' size='340' side='right'caption='[[2kac]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2kac]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"diplococcus_magnus"_prevot_1933 "diplococcus magnus" prevot 1933]. 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 [http://proteopedia.org/fgij/fg.htm?mol=2KAC FirstGlance]. <br> | + | <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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=2kac FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2kac OCA], [http://pdbe.org/2kac PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2kac RCSB], [http://www.ebi.ac.uk/pdbsum/2kac PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2kac ProSAT]</span></td></tr> | + | </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> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q51912_FINMA Q51912_FINMA] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Diplococcus magnus prevot 1933]] | + | [[Category: Finegoldia magna]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Lopez-Mendez, B]] | + | [[Category: Lopez-Mendez B]] |
| - | [[Category: Millet, O]] | + | [[Category: Millet O]] |
| - | [[Category: Pons, M]] | + | [[Category: Pons M]] |
| - | [[Category: Tadeo, X]] | + | [[Category: Tadeo X]] |
| - | [[Category: Cell wall]]
| + | |
| - | [[Category: Immune system]]
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| - | [[Category: Peptidoglycan-anchor]]
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| - | [[Category: Protein]]
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| Structural highlights
Function
Q51912_FINMA
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Tadeo X, Lopez-Mendez B, Trigueros T, Lain A, Castano D, Millet O. Structural basis for the aminoacid composition of proteins from halophilic archea. PLoS Biol. 2009 Dec;7(12):e1000257. Epub 2009 Dec 15. PMID:20016684 doi:10.1371/journal.pbio.1000257
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