3nep: Difference between revisions
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==1.55A resolution structure of malate dehydrogenase from Salinibacter ruber== | ==1.55A resolution structure of malate dehydrogenase from Salinibacter ruber== | ||
<StructureSection load='3nep' size='340' side='right' caption='[[3nep]], [[Resolution|resolution]] 1.55Å' scene=''> | <StructureSection load='3nep' size='340' side='right'caption='[[3nep]], [[Resolution|resolution]] 1.55Å' scene=''> | ||
== Structural highlights == | == 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:// | <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://proteopedia.org/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> | </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:// | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=3nep FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3nep OCA], [http://pdbe.org/3nep PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3nep RCSB], [http://www.ebi.ac.uk/pdbsum/3nep PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3nep ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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==See Also== | ==See Also== | ||
*[[Malate | *[[Malate Dehydrogenase 3D structures|Malate Dehydrogenase 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | |||
[[Category: Malate dehydrogenase]] | [[Category: Malate dehydrogenase]] | ||
[[Category: Salinibacter ruber]] | [[Category: Salinibacter ruber]] | ||
Revision as of 12:03, 21 October 2020
1.55A resolution structure of malate dehydrogenase from Salinibacter ruber1.55A resolution structure of malate dehydrogenase from Salinibacter ruber
Structural highlights
Function[MDH_SALRD] Catalyzes the reversible oxidation of malate to oxaloacetate.[HAMAP-Rule:MF_00487] 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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