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2zy4

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Revision as of 11:50, 12 October 2017

dodecameric L-aspartate beta-decarboxylase

Structural highlights

2zy4 is a 6 chain structure with sequence from 'alcaligenes odorans'. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Related:	2zy2, 2zy3, 2zy5
Gene:	asdA-AF ('Alcaligenes odorans')
Activity:	Aspartate 4-decarboxylase, with EC number 4.1.1.12
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[ASDA_COMTE] Bifunctional enzyme that has both L-aspartate decarboxylase and transaminase activity.^[1] [PDB:2ZY3]

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

The 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^[2]

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

References

↑ Chen HJ, Ko TP, Lee CY, Wang NC, Wang AH. Structure, assembly, and mechanism of a PLP-dependent dodecameric L-aspartate beta-decarboxylase. Structure. 2009 Apr 15;17(4):517-29. PMID:19368885 doi:10.1016/j.str.2009.02.013
↑ Chen HJ, Ko TP, Lee CY, Wang NC, Wang AH. Structure, assembly, and mechanism of a PLP-dependent dodecameric L-aspartate beta-decarboxylase. Structure. 2009 Apr 15;17(4):517-29. PMID:19368885 doi:10.1016/j.str.2009.02.013

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/2zy4"

@@ Line 1: / Line 1: @@
 ==dodecameric L-aspartate beta-decarboxylase==
 <StructureSection load='2zy4' size='340' side='right' caption='[[2zy4]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
@@ Line 7: / Line 8: @@
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">asdA-AF ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=32001 'Alcaligenes odorans'])</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Aspartate_4-decarboxylase Aspartate 4-decarboxylase], with EC number [http://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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2zy4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zy4 OCA], [http://pdbe.org/2zy4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2zy4 RCSB], [http://www.ebi.ac.uk/pdbsum/2zy4 PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2zy4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zy4 OCA], [http://pdbe.org/2zy4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2zy4 RCSB], [http://www.ebi.ac.uk/pdbsum/2zy4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2zy4 ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 30: / Line 31: @@
 </div>
 <div class="pdbe-citations 2zy4" style="background-color:#fffaf0;"></div>
-==See Also==
-*[[Aspartate decarboxylase|Aspartate decarboxylase]]
 == References ==
 <references/>

2zy4

From Proteopedia

Revision as of 11:50, 12 October 2017

dodecameric L-aspartate beta-decarboxylase

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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