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 [https://en.wikipedia.org/wiki/Salinibacter_ruber_DSM_13855 Salinibacter ruber DSM 13855]. 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 [https://proteopedia.org/fgij/fg.htm?mol=3NEP FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.551Å</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=3nep FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3nep OCA], [https://pdbe.org/3nep PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3nep RCSB], [https://www.ebi.ac.uk/pdbsum/3nep PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3nep ProSAT]</span></td></tr> | ||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/MDH_SALRD MDH_SALRD] Catalyzes the reversible oxidation of malate to oxaloacetate.[HAMAP-Rule:MF_00487] | |||
<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> | |||
<div class="pdbe-citations 3nep" style="background-color:#fffaf0;"></div> | |||
== | |||
==See Also== | ==See Also== | ||
*[[Malate | *[[Malate Dehydrogenase 3D structures|Malate Dehydrogenase 3D structures]] | ||
== References == | |||
== | <references/> | ||
< | __TOC__ | ||
[[Category: | </StructureSection> | ||
[[Category: Salinibacter ruber | [[Category: Large Structures]] | ||
[[Category: Coquelle | [[Category: Salinibacter ruber DSM 13855]] | ||
[[Category: Madern | [[Category: Coquelle N]] | ||
[[Category: Madern D]] | |||
Latest revision as of 12:14, 6 September 2023
1.55A resolution structure of malate dehydrogenase from Salinibacter ruber1.55A resolution structure of malate dehydrogenase from Salinibacter ruber
Structural highlights
FunctionMDH_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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