2C45

NATIVE PRECURSOR OF PYRUVOYL DEPENDENT ASPARTATE DECARBOXYLASE

Summary for 2C45

• Entry DOI: 10.2210/pdb2c45/pdb
• Descriptor: Aspartate 1-decarboxylase (2 entities in total)
• Functional Keywords: double-psi beta barrel, lyase, carboxylase, zymogen, pantothenate biosynthesis, decarboxylase, pyruvate
• Biological source: Mycobacterium tuberculosis
• Total number of polymer chains: 8
• Total formula weight: 119207.89

Authors

Gopalan, G.,Chopra, S.,Ranganathan, A.,Swaminathan, K. (deposition date: 2005-10-15, release date: 2007-03-06, Last modification date: 2023-12-13)

Primary citation

Gopalan, G.,Chopra, S.,Ranganathan, A.,Swaminathan, K.
Crystal structure of uncleaved L-aspartate-alpha-decarboxylase from Mycobacterium tuberculosis.
Proteins, 65:796-802, 2006

PubMed 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.

PubMed: 17001646
DOI: 10.1002/prot.21126

Experimental method

X-RAY DIFFRACTION (2.99 Å)