1bgv

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[[Image:1bgv.jpg|left|200px]]
 
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{{Structure
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==GLUTAMATE DEHYDROGENASE==
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|PDB= 1bgv |SIZE=350|CAPTION= <scene name='initialview01'>1bgv</scene>, resolution 1.9&Aring;
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<StructureSection load='1bgv' size='340' side='right'caption='[[1bgv]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=GLU:GLUTAMIC+ACID'>GLU</scene>
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<table><tr><td colspan='2'>[[1bgv]] 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=1BGV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BGV FirstGlance]. <br>
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|ACTIVITY= <span class='plainlinks'>[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] </span>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
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|GENE=
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GLU:GLUTAMIC+ACID'>GLU</scene></td></tr>
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|DOMAIN=
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1bgv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bgv OCA], [https://pdbe.org/1bgv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bgv RCSB], [https://www.ebi.ac.uk/pdbsum/1bgv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bgv ProSAT]</span></td></tr>
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|RELATEDENTRY=
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1bgv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bgv OCA], [http://www.ebi.ac.uk/pdbsum/1bgv PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1bgv RCSB]</span>
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== Function ==
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}}
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[https://www.uniprot.org/uniprot/DHE2_CLOSY DHE2_CLOSY]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bg/1bgv_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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=1bgv ConSurf].
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<div style="clear:both"></div>
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'''GLUTAMATE DEHYDROGENASE'''
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==See Also==
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*[[Glutamate dehydrogenase|Glutamate dehydrogenase]]
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*[[Glutamate dehydrogenase 3D structures|Glutamate dehydrogenase 3D structures]]
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==Overview==
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__TOC__
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We have solved the structure of the binary complex of the glutamate dehydrogenase from Clostridium symbiosum with glutamate to 1.9 A resolution. In this complex, the glutamate side-chain lies in a pocket on the enzyme surface and a key determinant of the enzymic specificity is an interaction of the substrate gamma-carboxyl group with the amino group of Lys89. In the apo-enzyme, Lys113 from the catalytic domain forms an important hydrogen bond to Asn373, in the NAD(+)-binding domain. On glutamate binding, the side-chain of this lysine undergoes a significant movement in order to optimize its hydrogen bonding to the alpha-carboxyl group of the substrate. Despite this shift, the interaction between Lys113 and Asn373 is maintained by a large-scale conformational change that closes the cleft between the two domains. Modelling studies indicate that in this "closed" conformation the C-4 of the nicotinamide ring and the alpha-carbon atom of the amino acid substrate are poised for efficient hydride transfer. Examination of the structure has led to a proposal for the catalytic activity of the enzyme, which involves Asp165 as a general base, and an enzyme-bound water molecule, hydrogen-bonded to an uncharged lysine residue, Lys125, as an attacking nucleophile in the reaction.
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</StructureSection>
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[[Category: Large Structures]]
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==About this Structure==
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[[Category: Baker PJ]]
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1BGV 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=1BGV OCA].
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[[Category: Britton KL]]
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[[Category: Rice DW]]
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==Reference==
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[[Category: Stillman TJ]]
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Conformational flexibility in glutamate dehydrogenase. Role of water in substrate recognition and catalysis., Stillman TJ, Baker PJ, Britton KL, Rice DW, J Mol Biol. 1993 Dec 20;234(4):1131-9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8263917 8263917]
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[[Category: Clostridium symbiosum]]
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[[Category: Glutamate dehydrogenase]]
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[[Category: Single protein]]
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[[Category: Baker, P J.]]
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[[Category: Britton, K L.]]
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[[Category: Rice, D W.]]
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[[Category: Stillman, T J.]]
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[[Category: oxidoreductase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:00:39 2008''
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Current revision

GLUTAMATE DEHYDROGENASE

PDB ID 1bgv

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