1kd0

From Proteopedia

(Difference between revisions)

Current revision

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

Structural highlights

1kd0 is a 2 chain structure with sequence from Clostridium tetanomorphum. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.9Å
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

MAAL_CLOTT

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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:11748244^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Asuncion M, Blankenfeldt W, Barlow JN, Gani D, Naismith JH. The structure of 3-methylaspartase from Clostridium tetanomorphum functions via the common enolase chemical step. J Biol Chem. 2002 Mar 8;277(10):8306-11. Epub 2001 Dec 17. PMID:11748244 doi:10.1074/jbc.M111180200

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1kd0"

@@ Line 3: / Line 3: @@
 <StructureSection load='1kd0' size='340' side='right'caption='[[1kd0]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1kd0]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/"clostridium_tetanomorphum"_bulloch_et_al._1919 "clostridium tetanomorphum" bulloch et al. 1919]. 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>
+<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>
-</td></tr><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></td></tr>
+</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>
-<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
+<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>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1kcz|1kcz]]</div></td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Methylaspartate_ammonia-lyase Methylaspartate ammonia-lyase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.3.1.2 4.3.1.2] </span></td></tr>
 <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>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/MAAL_CLOTT MAAL_CLOTT]
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 15: / Line 15: @@
   <jmolCheckbox>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/kd/1kd0_consurf.spt"</scriptWhenChecked>
-    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
@@ Line 33: / Line 33: @@
 __TOC__
 </StructureSection>
-[[Category: Clostridium tetanomorphum bulloch et al. 1919]]
+[[Category: Clostridium tetanomorphum]]
 [[Category: Large Structures]]
-[[Category: Methylaspartate ammonia-lyase]]
+[[Category: Asuncion M]]
-[[Category: Asuncion, M]]
+[[Category: Barlow JN]]
-[[Category: Barlow, J N]]
+[[Category: Blankenfeldt W]]
-[[Category: Blankenfeldt, W]]
+[[Category: Gani D]]
-[[Category: Gani, D]]
+[[Category: Naismith JH]]
-[[Category: Naismith, J H]]
-[[Category: Alpha/beta-barrel]]
-[[Category: Beta zigzag]]
-[[Category: Lyase]]

1kd0

From Proteopedia

Current revision

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

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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