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| | <StructureSection load='2hlp' size='340' side='right'caption='[[2hlp]], [[Resolution|resolution]] 2.59Å' scene=''> | | <StructureSection load='2hlp' size='340' side='right'caption='[[2hlp]], [[Resolution|resolution]] 2.59Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2hlp]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/"halobacterium_marismortui"_elazari-volcani_1957 "halobacterium marismortui" elazari-volcani 1957]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HLP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2HLP FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2hlp]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Haloarcula_marismortui Haloarcula marismortui]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HLP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2HLP FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.59Å</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Malate_dehydrogenase Malate dehydrogenase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.37 1.1.1.37] </span></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></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=2hlp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hlp OCA], [https://pdbe.org/2hlp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2hlp RCSB], [https://www.ebi.ac.uk/pdbsum/2hlp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2hlp ProSAT]</span></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=2hlp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hlp OCA], [https://pdbe.org/2hlp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2hlp RCSB], [https://www.ebi.ac.uk/pdbsum/2hlp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2hlp ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/MDH_HALMA MDH_HALMA]] Catalyzes the reversible oxidation of malate to oxaloacetate.[HAMAP-Rule:MF_00487]
| + | [https://www.uniprot.org/uniprot/MDH_HALMA MDH_HALMA] Catalyzes the reversible oxidation of malate to oxaloacetate.[HAMAP-Rule:MF_00487] |
| | == 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: Halobacterium marismortui elazari-volcani 1957]] | + | [[Category: Haloarcula marismortui]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Malate dehydrogenase]]
| + | [[Category: Garcin E]] |
| - | [[Category: Garcin, E]] | + | [[Category: Madern D]] |
| - | [[Category: Madern, D]] | + | [[Category: Richard SB]] |
| - | [[Category: Richard, S B]] | + | [[Category: Zaccai G]] |
| - | [[Category: Zaccai, G]] | + | |
| - | [[Category: Halophilic]]
| + | |
| - | [[Category: Ion-binding]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| - | [[Category: Salt bridge]]
| + | |
| Structural highlights
Function
MDH_HALMA Catalyzes the reversible oxidation of malate to oxaloacetate.[HAMAP-Rule:MF_00487]
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
Previous biophysical studies of tetrameric malate dehydrogenase from the halophilic archaeon Haloarcula marismortui (Hm MalDH) have revealed the importance of protein-solvent interactions for its adaptation to molar salt conditions that strongly affect protein solubility, stability, and activity, in general. The structures of the E267R stability mutant of apo (-NADH) Hm MalDH determined to 2.6 A resolution and of apo (-NADH) wild type Hm MalDH determined to 2.9 A resolution, presented here, highlight a variety of novel protein-solvent features involved in halophilic adaptation. The tetramer appears to be stabilized by ordered water molecule networks and intersubunit complex salt bridges "locked" in by bound solvent chloride and sodium ions. The E267R mutation points into a central ordered water cavity, disrupting protein-solvent interactions. The analysis of the crystal structures showed that halophilic adaptation is not aimed uniquely at "protecting" the enzyme from the extreme salt conditions, as may have been expected, but, on the contrary, consists of mechanisms that harness the high ionic concentration in the environment.
Halophilic adaptation: novel solvent protein interactions observed in the 2.9 and 2.6 A resolution structures of the wild type and a mutant of malate dehydrogenase from Haloarcula marismortui.,Richard SB, Madern D, Garcin E, Zaccai G Biochemistry. 2000 Feb 8;39(5):992-1000. PMID:10653643[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Richard SB, Madern D, Garcin E, Zaccai G. Halophilic adaptation: novel solvent protein interactions observed in the 2.9 and 2.6 A resolution structures of the wild type and a mutant of malate dehydrogenase from Haloarcula marismortui. Biochemistry. 2000 Feb 8;39(5):992-1000. PMID:10653643
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