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==dodecameric L-aspartate beta-decarboxylase== | ==dodecameric L-aspartate beta-decarboxylase== | ||
<StructureSection load='2zy2' size='340' side='right' caption='[[2zy2]], [[Resolution|resolution]] 3.30Å' scene=''> | <StructureSection load='2zy2' size='340' side='right'caption='[[2zy2]], [[Resolution|resolution]] 3.30Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2zy2]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[2zy2]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_sp._atcc_19121 Pseudomonas sp. atcc 19121]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZY2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ZY2 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2zy3|2zy3]], [[2zy4|2zy4]], [[2zy5|2zy5]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2zy3|2zy3]], [[2zy4|2zy4]], [[2zy5|2zy5]]</div></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">asdP ([ | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">asdP ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=206121 Pseudomonas sp. ATCC 19121])</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Aspartate_4-decarboxylase Aspartate 4-decarboxylase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.1.12 4.1.1.12] </span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2zy2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zy2 OCA], [https://pdbe.org/2zy2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2zy2 RCSB], [https://www.ebi.ac.uk/pdbsum/2zy2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2zy2 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[ | [[https://www.uniprot.org/uniprot/ASDP_PSESP ASDP_PSESP]] Bifunctional enzyme that has both L-aspartate decarboxylase and transaminase activity. Has high activity with L-aspartate, and much lower activity with D-aspartate, L-lysine and L-glutamine.<ref>PMID:16847601</ref> <ref>PMID:19368885</ref> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/zy/2zy2_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/zy/2zy2_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
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</div> | </div> | ||
<div class="pdbe-citations 2zy2" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 2zy2" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Aspartate decarboxylase 3D structures|Aspartate decarboxylase 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
| Line 36: | Line 39: | ||
</StructureSection> | </StructureSection> | ||
[[Category: Aspartate 4-decarboxylase]] | [[Category: Aspartate 4-decarboxylase]] | ||
[[Category: Large Structures]] | |||
[[Category: Pseudomonas sp. atcc 19121]] | [[Category: Pseudomonas sp. atcc 19121]] | ||
[[Category: Chen, H J]] | [[Category: Chen, H J]] | ||
Latest revision as of 19:10, 22 December 2021
dodecameric L-aspartate beta-decarboxylasedodecameric L-aspartate beta-decarboxylase
Structural highlights
Function[ASDP_PSESP] Bifunctional enzyme that has both L-aspartate decarboxylase and transaminase activity. Has high activity with L-aspartate, and much lower activity with D-aspartate, L-lysine and L-glutamine.[1] [2] 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 PubMedThe type-I PLP enzyme l-aspartate beta-decarboxylase converts aspartate to alanine and CO(2). Similar to the homodimeric aminotransferases, its protein subunit comprises a large and a small domain, of 410 and 120 residues, respectively. The crystal structure reveals a dodecamer made of six identical dimers arranged in a truncated tetrahedron whose assembly involves tetramer and hexamer as intermediates. The additional helical motifs I and II participate in the oligomer formation. Triple mutations of S67R/Y68R/M69R or S67E/Y68E/M69E in motif I produced an inactive dimer. The PLP is bound covalently to Lys315 in the active site, while its phosphate group interacts with a neighboring Tyr134. Removal of the bulky side chain of Arg37, which overhangs the PLP group, improved the substrate affinity. Mutations in flexible regions produced the more active K17A and the completely inactive R487A. The structure also suggests that substrate binding triggers conformational changes essential for catalyzing the reaction. Structure, assembly, and mechanism of a PLP-dependent dodecameric L-aspartate beta-decarboxylase.,Chen HJ, Ko TP, Lee CY, Wang NC, Wang AH Structure. 2009 Apr 15;17(4):517-29. PMID:19368885[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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