2zy5

R487A mutant of L-aspartate beta-decarboxylase

spinqualitylabelsall models 2zy5, resolution 2.65Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2zy5 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: PLP Related: 2zy2, 2zy3, 2zy4 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. [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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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