1hlp: Difference between revisions

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 ==STRUCTURAL FEATURES STABILIZING HALOPHILIC MALATE DEHYDROGENASE FROM AN ARCHAEBACTERIUM==
-<StructureSection load='1hlp' size='340' side='right' caption='[[1hlp]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
+<StructureSection load='1hlp' size='340' side='right'caption='[[1hlp]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1hlp]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"flavobacterium_(halobacterium)_maris-mortui_(sic)"_elazari-volcani_1940 "flavobacterium (halobacterium) maris-mortui (sic)" elazari-volcani 1940]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HLP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1HLP FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1hlp]] 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=1HLP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HLP FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</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]] 3.2&#8491;</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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene></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=1hlp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hlp OCA], [http://pdbe.org/1hlp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1hlp RCSB], [http://www.ebi.ac.uk/pdbsum/1hlp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1hlp 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=1hlp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hlp OCA], [https://pdbe.org/1hlp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hlp RCSB], [https://www.ebi.ac.uk/pdbsum/1hlp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hlp ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://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 ==
 [[Image:Consurf_key_small.gif|200px|right]]
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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=1hlp ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-The high-resolution structure of halophilic malate dehydrogenase (hMDH) from the archaebacterium Haloarcula marismortui was determined by x-ray crystallography. Comparison of the three-dimensional structures of hMDH and its nonhalophilic congeners reveals structural features that may promote the stability of hMDH at high salt concentrations. These features include an excess of acidic over basic residues distributed on the enzyme surface and more salt bridges present in hMDH compared with its nonhalophilic counterparts. Other features that contribute to the stabilization of thermophilic lactate dehydrogenase and thermophilic MDH-the incorporation of alanine into alpha helices and the introduction of negatively charged amino acids near their amino termini, both of which stabilize the alpha helix as a result of interaction with the positive part of the alpha-helix dipole-also were observed in hMDH.
-Structural Features That Stabilize Halophilic Malate Dehydrogenase from an Archaebacterium.,Dym O, Mevarech M, Sussman JL Science. 1995 Mar 3;267(5202):1344-1346. PMID:17812611<ref>PMID:17812611</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 1hlp" style="background-color:#fffaf0;"></div>
 ==See Also==
-*[[Halophilic malate dehydrogenase|Halophilic malate dehydrogenase]]
+*[[Malate Dehydrogenase 3D structures|Malate Dehydrogenase 3D structures]]
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: Malate dehydrogenase]]
+[[Category: Haloarcula marismortui]]
-[[Category: Dym, O]]
+[[Category: Large Structures]]
-[[Category: Mevarech, M]]
+[[Category: Dym O]]
-[[Category: Sussman, J L]]
+[[Category: Mevarech M]]
-[[Category: Dehydrogenase]]
+[[Category: Sussman JL]]
-[[Category: Halophilic]]