1d3a

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(New page: 200px<br /> <applet load="1d3a" size="450" color="white" frame="true" align="right" spinBox="true" caption="1d3a, resolution 2.94&Aring;" /> '''CRYSTAL STRUCTURE O...)
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[[Image:1d3a.gif|left|200px]]<br />
 
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<applet load="1d3a" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1d3a, resolution 2.94&Aring;" />
 
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'''CRYSTAL STRUCTURE OF THE WILD TYPE HALOPHILIC MALATE DEHYDROGENASE IN THE APO FORM'''<br />
 
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==Overview==
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==CRYSTAL STRUCTURE OF THE WILD TYPE HALOPHILIC MALATE DEHYDROGENASE IN THE APO FORM==
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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.
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<StructureSection load='1d3a' size='340' side='right'caption='[[1d3a]], [[Resolution|resolution]] 2.94&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1d3a]] 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=1D3A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1D3A FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.94&#8491;</td></tr>
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<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>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1d3a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1d3a OCA], [https://pdbe.org/1d3a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1d3a RCSB], [https://www.ebi.ac.uk/pdbsum/1d3a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1d3a ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/MDH_HALMA MDH_HALMA] Catalyzes the reversible oxidation of malate to oxaloacetate.[HAMAP-Rule:MF_00487]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/d3/1d3a_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1d3a ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1D3A is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Haloarcula_marismortui Haloarcula marismortui] with CL and NA as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1D3A OCA].
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*[[Malate Dehydrogenase 3D structures|Malate Dehydrogenase 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10653643 10653643]
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[[Category: Haloarcula marismortui]]
[[Category: Haloarcula marismortui]]
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[[Category: Malate dehydrogenase]]
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[[Category: Large Structures]]
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[[Category: Single protein]]
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[[Category: Garcin E]]
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[[Category: Garcin, E.]]
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[[Category: Madern D]]
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[[Category: Madern, D.]]
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[[Category: Richard SB]]
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[[Category: Richard, S.B.]]
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[[Category: Zaccai G]]
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[[Category: Zaccai, G.]]
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[[Category: CL]]
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[[Category: NA]]
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[[Category: rossmann fold and 3 sorts of complex salt bridges]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Thu Nov 8 12:38:42 2007''
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Current revision

CRYSTAL STRUCTURE OF THE WILD TYPE HALOPHILIC MALATE DEHYDROGENASE IN THE APO FORM

PDB ID 1d3a

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