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| - | [[Image:1aup.gif|left|200px]] | |
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| - | {{Structure
| + | ==GLUTAMATE DEHYDROGENASE== |
| - | |PDB= 1aup |SIZE=350|CAPTION= <scene name='initialview01'>1aup</scene>, resolution 2.5Å
| + | <StructureSection load='1aup' size='340' side='right'caption='[[1aup]], [[Resolution|resolution]] 2.50Å' scene=''> |
| - | |SITE=
| + | == Structural highlights == |
| - | |LIGAND=
| + | <table><tr><td colspan='2'>[[1aup]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Clostridium_symbiosum Clostridium symbiosum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AUP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AUP FirstGlance]. <br> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Glutamate_dehydrogenase Glutamate dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.1.2 1.4.1.2]
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5Å</td></tr> |
| - | |GENE= GDH ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1512 Clostridium symbiosum]) | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1aup FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1aup OCA], [https://pdbe.org/1aup PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1aup RCSB], [https://www.ebi.ac.uk/pdbsum/1aup PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1aup ProSAT]</span></td></tr> |
| - | }}
| + | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/DHE2_CLOSY DHE2_CLOSY] |
| | + | == Evolutionary Conservation == |
| | + | [[Image:Consurf_key_small.gif|200px|right]] |
| | + | Check<jmol> |
| | + | <jmolCheckbox> |
| | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/au/1aup_consurf.spt"</scriptWhenChecked> |
| | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> |
| | + | <text>to colour the structure by Evolutionary Conservation</text> |
| | + | </jmolCheckbox> |
| | + | </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=1aup ConSurf]. |
| | + | <div style="clear:both"></div> |
| | | | |
| - | '''GLUTAMATE DEHYDROGENASE'''
| + | ==See Also== |
| - | | + | *[[Glutamate dehydrogenase 3D structures|Glutamate dehydrogenase 3D structures]] |
| - | | + | __TOC__ |
| - | ==Overview== | + | </StructureSection> |
| - | The subunit of the enzyme glutamate dehydrogenase comprises two domains separated by a cleft harboring the active site. One domain is responsible for dinucleotide binding and the other carries the majority of residues which bind the substrate. During the catalytic cycle a large movement between the two domains occurs, closing the cleft and bringing the C4 of the nicotinamide ring and the Calpha of the substrate into the correct positioning for hydride transfer. In the active site, two residues, K89 and S380, make interactions with the gamma-carboxyl group of the glutamate substrate. In leucine dehydrogenase, an enzyme belonging to the same superfamily, the equivalent residues are L40 and V294, which create a more hydrophobic specificity pocket and provide an explanation for their differential substrate specificity. In an attempt to change the substrate specificity of glutamate dehydrogenase toward that of leucine dehydrogenase, a double mutant, K89L,S380V, of glutamate dehydrogenase has been constructed. Far from having a high specificity for leucine, this mutant appears to be devoid of any catalytic activity over a wide range of substrates tested. Determination of the three-dimensional structure of the mutant enzyme has shown that the loss of function is related to a disordering of residues linking the enzyme's two domains, probably arising from a steric clash between the valine side chain, introduced at position 380 in the mutant, and a conserved threonine residue, T193. In leucine dehydrogenase the steric clash between the equivalent valine and threonine side chains (V294, T134) does not occur owing to shifts of the main chain to which these side chains are attached. Thus, the differential substrate specificity seen in the amino acid dehydrogenase superfamily arises from both the introduction of simple point mutations and the fine tuning of the active site pocket defined by small but significant main chain rearrangements.
| + | [[Category: Large Structures]] |
| - | | + | [[Category: Baker PJ]] |
| - | ==About this Structure==
| + | [[Category: Rice DW]] |
| - | 1AUP is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Clostridium_symbiosum Clostridium symbiosum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AUP OCA].
| + | [[Category: Stillman TJ]] |
| - | | + | [[Category: Turnbull AP]] |
| - | ==Reference==
| + | [[Category: Waugh ML]] |
| - | Determinants of substrate specificity in the superfamily of amino acid dehydrogenases., Baker PJ, Waugh ML, Wang XG, Stillman TJ, Turnbull AP, Engel PC, Rice DW, Biochemistry. 1997 Dec 23;36(51):16109-15. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9405044 9405044]
| + | |
| - | [[Category: Clostridium symbiosum]] | + | |
| - | [[Category: Glutamate dehydrogenase]]
| + | |
| - | [[Category: Single protein]]
| + | |
| - | [[Category: Baker, P J.]] | + | |
| - | [[Category: Rice, D W.]] | + | |
| - | [[Category: Stillman, T J.]] | + | |
| - | [[Category: Turnbull, A P.]] | + | |
| - | [[Category: Waugh, M L.]] | + | |
| - | [[Category: nad]]
| + | |
| - | [[Category: oxidoreductase]]
| + | |
| - | | + | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:02:29 2008''
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