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| <StructureSection load='4jco' size='340' side='right'caption='[[4jco]], [[Resolution|resolution]] 1.70Å' scene=''> | | <StructureSection load='4jco' size='340' side='right'caption='[[4jco]], [[Resolution|resolution]] 1.70Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
| <table><tr><td colspan='2'>[[4jco]] is a 4 chain structure with sequence from [http://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=4JCO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4JCO FirstGlance]. <br> | | <table><tr><td colspan='2'>[[4jco]] is a 4 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=4JCO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4JCO FirstGlance]. <br> |
| </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> | | </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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1d3a|1d3a]], [[1gt2|1gt2]], [[1hlp|1hlp]], [[1o6z|1o6z]], [[2hlp|2hlp]], [[2j5k|2j5k]], [[2j5q|2j5q]], [[2j5r|2j5r]]</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=4jco FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4jco OCA], [https://pdbe.org/4jco PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4jco RCSB], [https://www.ebi.ac.uk/pdbsum/4jco PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4jco ProSAT]</span></td></tr> |
| <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">mdh, rrnAC2706 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2238 "Halobacterium marismortui" Elazari-Volcani 1957])</td></tr>
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| <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>
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| <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=4jco FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4jco OCA], [http://pdbe.org/4jco PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4jco RCSB], [http://www.ebi.ac.uk/pdbsum/4jco PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4jco ProSAT]</span></td></tr> | |
| </table> | | </table> |
| == Function == | | == 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] |
| <div style="background-color:#fffaf0;">
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| == Publication Abstract from PubMed ==
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| Intense synchrotron radiation produces specific structural and chemical damage to crystalline proteins even at 100 K. Carboxyl groups of acidic residues (Glu, Asp) losing their definition is one of the major effects observed. Here, the susceptibilities to X-ray damage of acidic residues in tetrameric malate dehydrogenase from Haloarcula marismortui are investigated. The marked excess of acidic residues in this halophilic enzyme makes it an ideal target to determine how specific damage to acidic residues is related to their structural and chemical environment. Four conclusions are drawn. (i) Acidic residues interacting with the side-chains of lysine and arginine residues are less affected by radiation damage than those interacting with serine, threonine and tyrosine side-chains. This suggests that residues with higher pK(a) values are more vulnerable to damage than those with a lower pK(a). However, such a correlation was not found when calculated pK(a) values were inspected. (ii) Acidic side-chains located in the enzymatic active site are the most radiation-sensitive ones. (iii) Acidic residues in the internal cavity formed by the four monomers and those involved in crystal contacts appear to be particularly susceptible. (iv) No correlation was found between radiation susceptibility and solvent accessibility.
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| Specific radiation damage to acidic residues and its relation to their chemical and structural environment.,Fioravanti E, Vellieux FM, Amara P, Madern D, Weik M J Synchrotron Radiat. 2007 Jan;14(Pt 1):84-91. Epub 2006 Dec 15. PMID:17211074<ref>PMID:17211074</ref>
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| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| </div>
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| <div class="pdbe-citations 4jco" style="background-color:#fffaf0;"></div>
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| ==See Also== | | ==See Also== |
| *[[Malate Dehydrogenase 3D structures|Malate Dehydrogenase 3D structures]] | | *[[Malate Dehydrogenase 3D structures|Malate Dehydrogenase 3D structures]] |
| == References ==
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| <references/>
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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: Vellieux FMD]] |
| [[Category: Vellieux, F M.D]] | |
| [[Category: Halophile]]
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| [[Category: Malate dehydrogenase tricarboxylic acid cycle]]
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| [[Category: Oxidoreductase]]
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