5ls7 | pdb_00005ls7

Complex of wild type E. coli alpha aspartate decarboxylase with its processing factor PanZ

spinqualitylabelsall models 5ls7, resolution 1.16Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5ls7 is a 3 chain structure with sequence from Escherichia coli K-12. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.16Å Ligands: 74C, ACO, CO2, CSO, GOL, MG, PEG, PVO, SCN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function PAND_ECOLI Catalyzes the pyruvoyl-dependent decarboxylation of aspartate to produce beta-alanine. Publication Abstract from PubMed The antimetabolite pentyl pantothenamide has broad spectrum antibiotic activity but exhibits enhanced activity against Escherichia coli. The PanDZ complex has been proposed to regulate the pantothenate biosynthetic pathway in E. coli by limiting the supply of beta-alanine in response to coenzyme A concentration. We show that formation of such a complex between activated aspartate decarboxylase (PanD) and PanZ leads to sequestration of the pyruvoyl cofactor as a ketone hydrate and demonstrate that both PanZ overexpression-linked beta-alanine auxotrophy and pentyl pantothenamide toxicity are due to formation of this complex. This both demonstrates that the PanDZ complex regulates pantothenate biosynthesis in a cellular context and validates the complex as a target for antibiotic development. The Mechanism of Regulation of Pantothenate Biosynthesis by the PanD-PanZ.AcCoA Complex Reveals an Additional Mode of Action for the Antimetabolite N-Pentyl Pantothenamide (N5-Pan).,Arnott ZLP, Nozaki S, Monteiro DCF, Morgan HE, Pearson AR, Niki H, Webb ME Biochemistry. 2017 Sep 7. doi: 10.1021/acs.biochem.7b00509. PMID:28832133 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Aspartate decarboxylase 3D structures

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