2C45: NATIVE PRECURSOR OF PYRUVOYL DEPENDENT ASPARTATE DECARBOXYLASE

Citation:
Abstract
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.
PDB ID: 2C45Download
MMDB ID: 44285
PDB Deposition Date: 2005/10/15
Updated in MMDB: 2007/10
Experimental Method:
x-ray diffraction
Resolution: 2.99  Å
Similar Structures:
Biological Unit for 2C45: tetrameric; determined by author and by software (PQS)
Molecular Components in 2C45
Label Count Molecule
Proteins (4 molecules)
4
Aspartate 1-decarboxylase Precursor
Molecule annotation
* Click molecule labels to explore molecular sequence information.

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