1dgj

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(New page: 200px<br /><applet load="1dgj" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dgj, resolution 2.8&Aring;" /> '''CRYSTAL STRUCTURE OF ...)
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[[Image:1dgj.jpg|left|200px]]<br /><applet load="1dgj" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1dgj, resolution 2.8&Aring;" />
 
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'''CRYSTAL STRUCTURE OF THE ALDEHYDE OXIDOREDUCTASE FROM DESULFOVIBRIO DESULFURICANS ATCC 27774'''<br />
 
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==Overview==
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==CRYSTAL STRUCTURE OF THE ALDEHYDE OXIDOREDUCTASE FROM DESULFOVIBRIO DESULFURICANS ATCC 27774==
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The aldehyde oxidoreductase (MOD) isolated from the sulfate reducer, Desulfovibrio desulfuricans (ATCC 27774) is a member of the xanthine, oxidase family of molybdenum-containing enzymes. It has substrate, specificity similar to that of the homologous enzyme from Desulfovibrio, gigas (MOP) and the primary sequences from both enzymes show 68 %, identity. The enzyme was crystallized in space group P6(1)22, with unit, cell dimensions of a=b=156.4 A and c=177.1 A, and diffraction data were, obtained to beyond 2.8 A. The crystal structure was solved by Patterson, search techniques using the coordinates of the D. gigas enzyme. The, overall fold of the D. desulfuricans enzyme is very similar to MOP and the, few differences are mapped to exposed regions of the molecule. This is, reflected in the electrostatic potential surfaces of both homologous, enzymes, one exception being the surface potential in a region, identifiable as the putative docking site of the physiological electron, acceptor. Other essential features of the MOP structure, such as residues, of the active-site cavity, are basically conserved in MOD. Two mutations, are located in the pocket bearing a chain of catalytically relevant water, molecules.As deduced from this work, both these enzymes are very closely, related in terms of their sequences as well as 3D structures. The, comparison allowed confirmation and establishment of features that are, essential for their function; namely, conserved residues in the, active-site, catalytically relevant water molecules and recognition of the, physiological electron acceptor docking site.
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<StructureSection load='1dgj' size='340' side='right'caption='[[1dgj]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[1dgj]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Desulfovibrio_desulfuricans Desulfovibrio desulfuricans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DGJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DGJ FirstGlance]. <br>
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1DGJ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Desulfovibrio_desulfuricans Desulfovibrio desulfuricans] with FES, 2MO and MCN as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1DGJ OCA].
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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]] 2.8&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=2MO:MOLYBDENUM+(IV)OXIDE'>2MO</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=MCN:PTERIN+CYTOSINE+DINUCLEOTIDE'>MCN</scene></td></tr>
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==Reference==
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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=1dgj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dgj OCA], [https://pdbe.org/1dgj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dgj RCSB], [https://www.ebi.ac.uk/pdbsum/1dgj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dgj ProSAT]</span></td></tr>
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Gene sequence and crystal structure of the aldehyde oxidoreductase from Desulfovibrio desulfuricans ATCC 27774., Rebelo J, Macieira S, Dias JM, Huber R, Ascenso CS, Rusnak F, Moura JJ, Moura I, Romao MJ, J Mol Biol. 2000 Mar 17;297(1):135-46. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10704312 10704312]
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/Q9REC4_DESDE Q9REC4_DESDE]
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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/dg/1dgj_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=1dgj ConSurf].
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<div style="clear:both"></div>
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__TOC__
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</StructureSection>
[[Category: Desulfovibrio desulfuricans]]
[[Category: Desulfovibrio desulfuricans]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Dias, J.M.]]
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[[Category: Dias JM]]
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[[Category: Huber, R.]]
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[[Category: Huber R]]
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[[Category: Macieira, S.]]
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[[Category: Macieira S]]
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[[Category: Rebelo, J.M.]]
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[[Category: Rebelo JM]]
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[[Category: Romao, M.J.]]
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[[Category: Romao MJ]]
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[[Category: 2MO]]
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[[Category: FES]]
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[[Category: MCN]]
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[[Category: beta barrel]]
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[[Category: beta half-barrel]]
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[[Category: four-helix bundle]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 03:06:37 2007''
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Current revision

CRYSTAL STRUCTURE OF THE ALDEHYDE OXIDOREDUCTASE FROM DESULFOVIBRIO DESULFURICANS ATCC 27774

PDB ID 1dgj

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