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| | ==1.70 A resolution structure of the malate dehydrogenase from Chloroflexus aurantiacus== | | ==1.70 A resolution structure of the malate dehydrogenase from Chloroflexus aurantiacus== |
| - | <StructureSection load='4cl3' size='340' side='right' caption='[[4cl3]], [[Resolution|resolution]] 1.70Å' scene=''> | + | <StructureSection load='4cl3' size='340' side='right'caption='[[4cl3]], [[Resolution|resolution]] 1.70Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4cl3]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Chloroflexus_sp._y-400-fl Chloroflexus sp. y-400-fl]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=4bgt 4bgt]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CL3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4CL3 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4cl3]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Chloroflexus_aurantiacus_Y-400-fl Chloroflexus aurantiacus Y-400-fl]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=4bgt 4bgt]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CL3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4CL3 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CD:CADMIUM+ION'>CD</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CD:CADMIUM+ION'>CD</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4bgu|4bgu]], [[4bgv|4bgv]]</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=4cl3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cl3 OCA], [https://pdbe.org/4cl3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4cl3 RCSB], [https://www.ebi.ac.uk/pdbsum/4cl3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4cl3 ProSAT]</span></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>
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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=4cl3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cl3 OCA], [http://pdbe.org/4cl3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4cl3 RCSB], [http://www.ebi.ac.uk/pdbsum/4cl3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4cl3 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/MDH_CHLSY MDH_CHLSY]] Catalyzes the reversible oxidation of malate to oxaloacetate (By similarity). | + | [[https://www.uniprot.org/uniprot/MDH_CHLSY MDH_CHLSY]] Catalyzes the reversible oxidation of malate to oxaloacetate (By similarity). |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | ==See Also== | | ==See Also== |
| - | *[[Malate dehydrogenase|Malate dehydrogenase]] | + | *[[Malate Dehydrogenase 3D structures|Malate Dehydrogenase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Chloroflexus sp. y-400-fl]] | + | [[Category: Chloroflexus aurantiacus Y-400-fl]] |
| - | [[Category: Malate dehydrogenase]] | + | [[Category: Large Structures]] |
| - | [[Category: Girard, E]] | + | [[Category: Girard E]] |
| - | [[Category: Madern, D]] | + | [[Category: Madern D]] |
| - | [[Category: Talon, R]] | + | [[Category: Talon R]] |
| - | [[Category: Oxidoreductase]]
| + | |
| - | [[Category: Thermophile]]
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| - | [[Category: Tricarboxylic acid cycle]]
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| Structural highlights
Function
[MDH_CHLSY] Catalyzes the reversible oxidation of malate to oxaloacetate (By similarity).
Publication Abstract from PubMed
Protein-solvent interactions govern the behaviors of proteins isolated from extreme halophiles. In this work, we compared the solvent envelopes of two orthologous tetrameric malate dehydrogenases (MalDHs) from halophilic and non-halophilic bacteria. The crystal structure of the MalDH from the non-halophilic bacterium Chloroflexus aurantiacus (Ca MalDH) solved, de novo, at 1.7 A resolution exhibits numerous water molecules in its solvation shell. We observed that a large number of these water molecules are arranged in pentagonal polygons in the first hydration shell of Ca MalDH. Some of them are clustered in large networks, which cover non-polar amino acid surface. The crystal structure of MalDH from the extreme halophilic bacterium Salinibacter ruber (Sr) solved at 1.55 A resolution shows that its surface is strongly enriched in acidic amino acids. The structural comparison of these two models is the first direct observation of the relative impact of acidic surface enrichment on the water structure organization between a halophilic protein and its non-adapted counterpart. The data show that surface acidic amino acids disrupt pentagonal water networks in the hydration shell. These crystallographic observations are discussed with respect to halophilic protein behaviors in solution.
An experimental point of view on hydration/solvation in halophilic proteins.,Talon R, Coquelle N, Madern D, Girard E Front Microbiol. 2014 Feb 21;5:66. doi: 10.3389/fmicb.2014.00066. eCollection, 2014. PMID:24600446[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Talon R, Coquelle N, Madern D, Girard E. An experimental point of view on hydration/solvation in halophilic proteins. Front Microbiol. 2014 Feb 21;5:66. doi: 10.3389/fmicb.2014.00066. eCollection, 2014. PMID:24600446 doi:http://dx.doi.org/10.3389/fmicb.2014.00066
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