3nep: Difference between revisions
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[[ | ==1.55A resolution structure of malate dehydrogenase from Salinibacter ruber== | ||
<StructureSection load='3nep' size='340' side='right' caption='[[3nep]], [[Resolution|resolution]] 1.55Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3nep]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Salinibacter_ruber Salinibacter ruber]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3NEP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3NEP FirstGlance]. <br> | |||
</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Malate_dehydrogenase Malate dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.37 1.1.1.37] </span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3nep FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3nep OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3nep RCSB], [http://www.ebi.ac.uk/pdbsum/3nep PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Several experimental techniques were applied to unravel fine molecular details of protein adaptation to high salinity. We compared four homologous enzymes, which suggested a new halo-adaptive state in the process of molecular adaptation to high-salt conditions. Together with comparative functional studies, the structure of malate dehydrogenase from the eubacterium Salinibacter ruber shows that the enzyme shares characteristics of a halo-adapted archaea-bacterial enzyme and of non-halo-adapted enzymes from other eubacterial species. The S. ruber enzyme is active at the high physiological concentrations of KCl but, unlike typical halo-adapted enzymes, remains folded and active at low salt concentrations. Structural aspects of the protein, including acidic residues at the surface, solvent-exposed hydrophobic surface, and buried hydrophobic surface, place it between the typical halo-adapted and non-halo-adapted proteins. The enzyme lacks inter-subunit ion-binding sites often seen in halo-adapted enzymes. These observations permit us to suggest an evolutionary pathway that is highlighted by subtle trade-offs to achieve an optimal compromise among solubility, stability, and catalytic activity. | |||
Gradual Adaptive Changes of a Protein Facing High Salt Concentrations.,Coquelle N, Talon R, Juers DH, Girard E, Kahn R, Madern D J Mol Biol. 2010 Oct 1. PMID:20888835<ref>PMID:20888835</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
==See Also== | ==See Also== | ||
*[[Malate dehydrogenase|Malate dehydrogenase]] | *[[Malate dehydrogenase|Malate dehydrogenase]] | ||
== References == | |||
== | <references/> | ||
< | __TOC__ | ||
</StructureSection> | |||
[[Category: Malate dehydrogenase]] | [[Category: Malate dehydrogenase]] | ||
[[Category: Salinibacter ruber]] | [[Category: Salinibacter ruber]] | ||
[[Category: Coquelle, N | [[Category: Coquelle, N]] | ||
[[Category: Madern, D | [[Category: Madern, D]] | ||
[[Category: Halophile]] | [[Category: Halophile]] | ||
[[Category: Molecular adpatation]] | [[Category: Molecular adpatation]] | ||
[[Category: Nad]] | [[Category: Nad]] | ||
[[Category: Oxidoreductase]] | [[Category: Oxidoreductase]] | ||
[[Category: Tricarboxylic acid cycle]] | [[Category: Tricarboxylic acid cycle]] | ||
Revision as of 21:12, 21 December 2014
1.55A resolution structure of malate dehydrogenase from Salinibacter ruber1.55A resolution structure of malate dehydrogenase from Salinibacter ruber
Structural highlights
Publication Abstract from PubMedSeveral experimental techniques were applied to unravel fine molecular details of protein adaptation to high salinity. We compared four homologous enzymes, which suggested a new halo-adaptive state in the process of molecular adaptation to high-salt conditions. Together with comparative functional studies, the structure of malate dehydrogenase from the eubacterium Salinibacter ruber shows that the enzyme shares characteristics of a halo-adapted archaea-bacterial enzyme and of non-halo-adapted enzymes from other eubacterial species. The S. ruber enzyme is active at the high physiological concentrations of KCl but, unlike typical halo-adapted enzymes, remains folded and active at low salt concentrations. Structural aspects of the protein, including acidic residues at the surface, solvent-exposed hydrophobic surface, and buried hydrophobic surface, place it between the typical halo-adapted and non-halo-adapted proteins. The enzyme lacks inter-subunit ion-binding sites often seen in halo-adapted enzymes. These observations permit us to suggest an evolutionary pathway that is highlighted by subtle trade-offs to achieve an optimal compromise among solubility, stability, and catalytic activity. Gradual Adaptive Changes of a Protein Facing High Salt Concentrations.,Coquelle N, Talon R, Juers DH, Girard E, Kahn R, Madern D J Mol Biol. 2010 Oct 1. PMID:20888835[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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