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1kd0

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(New page: 200px<br /><applet load="1kd0" size="450" color="white" frame="true" align="right" spinBox="true" caption="1kd0, resolution 1.90&Aring;" /> '''Crystal Structure of...)
Current revision (07:59, 3 April 2024) (edit) (undo)
 
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[[Image:1kd0.jpg|left|200px]]<br /><applet load="1kd0" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1kd0, resolution 1.90&Aring;" />
 
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'''Crystal Structure of beta-methylaspartase from Clostridium tetanomorphum. Apo-structure.'''<br />
 
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==Overview==
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==Crystal Structure of beta-methylaspartase from Clostridium tetanomorphum. Apo-structure.==
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Methylaspartate ammonia-lyase (3-methylaspartase, MAL; EC ) catalyzes the, reversible anti elimination of ammonia from, L-threo-(2S,3S)-3-methylaspartic acid to give mesaconic acid. This, reaction lies on the main catabolic pathway for glutamate in Clostridium, tetanomorphum. MAL requires monovalent and divalent cation cofactors for, full catalytic activity. The enzyme has attracted interest because of its, potential use as a biocatalyst. The structure of C. tetanomorphum MAL has, been solved to 1.9-A resolution by the single-wavelength anomalous, diffraction method. A divalent metal ion complex of the protein has also, been determined. MAL is a homodimer with each monomer consisting of two, domains. One is an alpha/beta-barrel, and the other smaller domain is, mainly beta-strands. The smaller domain partially occludes the C terminus, of the barrel and forms a large cleft. The structure identifies MAL as, belonging to the enolase superfamily of enzymes. The metal ion site is, located in a large cleft between the domains. Potential active site, residues have been identified based on a combination of their proximity to, a metal ion site, molecular modeling, and sequence homology. In common, with all members of the enolase superfamily, the carboxylic acid of the, substrate is co-ordinated by the metal ions, and a proton adjacent to a, carboxylic acid group of the substrate is abstracted by a base. In MAL, it, appears that Lys(331) removes the alpha-proton of methylaspartic acid., This motif is the defining mechanistic characteristic of the enolase, superfamily of which all have a common fold. The degree of structural, conservation is remarkable given only four residues are absolutely, conserved.
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<StructureSection load='1kd0' size='340' side='right'caption='[[1kd0]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[1kd0]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Clostridium_tetanomorphum Clostridium tetanomorphum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KD0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KD0 FirstGlance]. <br>
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1KD0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Clostridium_tetanomorphum Clostridium tetanomorphum] with EDO as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Methylaspartate_ammonia-lyase Methylaspartate ammonia-lyase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.3.1.2 4.3.1.2] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1KD0 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]] 1.9&#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=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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=1kd0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kd0 OCA], [https://pdbe.org/1kd0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1kd0 RCSB], [https://www.ebi.ac.uk/pdbsum/1kd0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1kd0 ProSAT]</span></td></tr>
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The structure of 3-methylaspartase from Clostridium tetanomorphum functions via the common enolase chemical step., Asuncion M, Blankenfeldt W, Barlow JN, Gani D, Naismith JH, J Biol Chem. 2002 Mar 8;277(10):8306-11. Epub 2001 Dec 17. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11748244 11748244]
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/MAAL_CLOTT MAAL_CLOTT]
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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/kd/1kd0_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=1kd0 ConSurf].
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<div style="clear:both"></div>
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__TOC__
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</StructureSection>
[[Category: Clostridium tetanomorphum]]
[[Category: Clostridium tetanomorphum]]
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[[Category: Methylaspartate ammonia-lyase]]
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[[Category: Large Structures]]
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[[Category: Single protein]]
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[[Category: Asuncion M]]
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[[Category: Asuncion, M.]]
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[[Category: Barlow JN]]
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[[Category: Barlow, J.N.]]
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[[Category: Blankenfeldt W]]
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[[Category: Blankenfeldt, W.]]
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[[Category: Gani D]]
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[[Category: Gani, D.]]
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[[Category: Naismith JH]]
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[[Category: Naismith, J.H.]]
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[[Category: EDO]]
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[[Category: alpha/beta-barrel]]
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[[Category: beta zigzag]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 19:04:15 2007''
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Current revision

Crystal Structure of beta-methylaspartase from Clostridium tetanomorphum. Apo-structure.

PDB ID 1kd0

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