2c45
From Proteopedia
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NATIVE PRECURSOR OF PYRUVOYL DEPENDENT ASPARTATE DECARBOXYLASE
Overview
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.
About this Structure
2C45 is a Single protein structure of sequence from [1]. Active as Aspartate 1-decarboxylase, with EC number 4.1.1.11 Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Wed Nov 21 09:00:16 2007
