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| - | | + | #REDIRECT [[6dhn]] This PDB entry is obsolete and replaced by 6dhn |
| - | ==Crystal structure of bovine glutamate dehydrogenase complexed with Eu3+==
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| - | <StructureSection load='3mvo' size='340' side='right' caption='[[3mvo]], [[Resolution|resolution]] 3.23Å' scene=''>
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| - | == Structural highlights ==
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| - | <table><tr><td colspan='2'>[[3mvo]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3MVO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3MVO FirstGlance]. <br>
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| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EU3:EUROPIUM+(III)+ION'>EU3</scene>, <scene name='pdbligand=GLU:GLUTAMIC+ACID'>GLU</scene>, <scene name='pdbligand=NDP:NADPH+DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NDP</scene></td></tr>
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| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1hwz|1hwz]], [[3mvq|3mvq]]</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/Glutamate_dehydrogenase_(NAD(P)(+)) Glutamate dehydrogenase (NAD(P)(+))], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.1.3 1.4.1.3] </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=3mvo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mvo OCA], [http://pdbe.org/3mvo PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3mvo RCSB], [http://www.ebi.ac.uk/pdbsum/3mvo PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3mvo ProSAT]</span></td></tr>
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| - | </table>
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| - | == Function ==
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| - | [[http://www.uniprot.org/uniprot/DHE3_BOVIN DHE3_BOVIN]] May be involved in learning and memory reactions by increasing the turnover of the excitatory neurotransmitter glutamate (By similarity).<ref>PMID:14659072</ref>
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| - | <div style="background-color:#fffaf0;">
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| - | == Publication Abstract from PubMed ==
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| - | Bovine glutamate dehydrogenase is potently inhibited by zinc and the major impact is on V(max) suggesting a V-type effect on catalysis or product release. Zinc inhibition decreases as glutamate concentrations decrease suggesting a role for subunit interactions. With the monocarboxylic amino acid norvaline, which gives no evidence of subunit interactions, zinc does not inhibit. Zinc significantly decreases the size of the pre-steady state burst in the reaction but does not affect NADPH binding in the enzyme-NADPH-glutamate complex that governs the steady state turnover, again suggesting that zinc disrupts subunit interactions required for catalytic competence. While differential scanning calorimetry suggests zinc binds and induces a slightly conformationally more rigid state of the protein, limited proteolysis indicates that regions in the vicinity of the antennae regions and the trimer-trimer interface become more flexible. The structures of glutamate dehydrogenase bound with zinc and europium show that zinc binds between the three dimers of subunits in the hexamer, a region shown to bind novel inhibitors that block catalytic turnover, which is consistent with the above findings. In contrast, europium binds to the base of the antenna region and appears to abrogate the inhibitory effect of zinc. Structures of various states of the enzyme have shown that both regions are heavily involved in the conformational changes associated with catalytic turnover. These results suggest that the V-type inhibition produced with glutamate as the substrate results from disruption of subunit interactions necessary for efficient catalysis rather than by a direct effect on the active site conformation. Structured digital abstract * GHD binds to GHD by x-ray crystallography (View interaction).
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| - | A novel mechanism of V-type zinc inhibition of glutamate dehydrogenase results from disruption of subunit interactions necessary for efficient catalysis.,Bailey J, Powell L, Sinanan L, Neal J, Li M, Smith T, Bell E FEBS J. 2011 Sep;278(17):3140-51. doi: 10.1111/j.1742-4658.2011.08240.x., Epub 2011 Aug 11. PMID:21749647<ref>PMID:21749647</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 3mvo" style="background-color:#fffaf0;"></div>
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| - | ==See Also==
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| - | *[[Glutamate dehydrogenase|Glutamate dehydrogenase]]
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| - | == References ==
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| - | <references/>
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| - | __TOC__
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| - | </StructureSection>
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| - | [[Category: Bos taurus]]
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| - | [[Category: Li, M]]
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| - | [[Category: Smith, T J]]
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| - | [[Category: Eu3+]]
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| - | [[Category: Gdh]]
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| - | [[Category: Glutamate dehydrogenase]]
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| - | [[Category: Oxidoreductase]]
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