2C45

NATIVE PRECURSOR OF PYRUVOYL DEPENDENT ASPARTATE DECARBOXYLASE

2C45 の概要

• エントリーDOI: 10.2210/pdb2c45/pdb
• 分子名称: Aspartate 1-decarboxylase (2 entities in total)
• 機能のキーワード: double-psi beta barrel, lyase, carboxylase, zymogen, pantothenate biosynthesis, decarboxylase, pyruvate
• 由来する生物種: Mycobacterium tuberculosis
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 119207.89

構造登録者

Gopalan, G.,Chopra, S.,Ranganathan, A.,Swaminathan, K. (登録日: 2005-10-15, 公開日: 2007-03-06, 最終更新日: 2023-12-13)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.99 Å)