2c45

NATIVE PRECURSOR OF PYRUVOYL DEPENDENT ASPARTATE DECARBOXYLASE

spinqualitylabelsall models 2c45, resolution 2.99Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2c45 is a 8 chain structure with sequence from "bacillus_tuberculosis"_(zopf_1883)_klein_1884 "bacillus tuberculosis" (zopf 1883) klein 1884. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Gene: panD, Rv3601c, MTCY07H7B.21 ("Bacillus tuberculosis" (Zopf 1883) Klein 1884) Activity: Aspartate 1-decarboxylase, with EC number 4.1.1.11 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [PAND_MYCTU] Catalyzes the pyruvoyl-dependent decarboxylation of aspartate to produce beta-alanine (By similarity). 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 L-aspartate-alpha-decarboxylase (ADC) is a critical regulatory enzyme in the pantothenate biosynthetic pathway and belongs to a small class of self-cleaving and pyruvoyl-dependent amino acid decarboxylases. The expression level of ADC in Mycobacterium tuberculosis (Mtb) was confirmed by cDNA analysis, immunoblotting with an anti-ADC polyclonal antibody using whole cell lysate and immunoelectron microscopy. The recombinant ADC proenzyme from Mycobacterium tuberculosis (MtbADC) was overexpressed in E. coli and the protein structure was determined at 2.99 A resolution. The proteins fold into the double-psi beta-barrel structure. The subunits of the two tetramers (there are eight ADC molecules in the asymmetric unit) form pseudo fourfold rotational symmetry, similar to the E. coli ADC proenzyme structure. As pantothenate is synthesized in microorganisms, plants, and fungi but not in animals, structure elucidation of Mtb ADC is of substantial interest for structure-based drug development. Crystal structure of uncleaved L-aspartate-alpha-decarboxylase from Mycobacterium tuberculosis.,Gopalan G, Chopra S, Ranganathan A, Swaminathan K Proteins. 2006 Dec 1;65(4):796-802. PMID:17001646 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Aspartate decarboxylase 3D structures

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