3DBO

Crystal structure of a member of the VapBC family of toxin-antitoxin systems, VapBC-5, from Mycobacterium tuberculosis

3DBO の概要

• エントリーDOI: 10.2210/pdb3dbo/pdb
• 分子名称: Uncharacterized protein, SODIUM ION, ACETATE ION, ... (6 entities in total)
• 機能のキーワード: toxin antitoxin complex, vapbc, mycobacterium tuberculosis, structural genomics, psi-2, protein structure initiative, integrated center for structure and function innovation, isfi, tb structural genomics consortium, tbsgc, toxin-antitoxin complex, toxin/antitoxin
• 由来する生物種: Mycobacterium tuberculosis; 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 26648.12

構造登録者

Miallau, L.,Cascio, D.,Eisenberg, D.,Integrated Center for Structure and Function Innovation (ISFI),TB Structural Genomics Consortium (TBSGC) (登録日: 2008-06-02, 公開日: 2008-07-15, 最終更新日: 2024-02-21)

主引用文献

Miallau, L.,Faller, M.,Chiang, J.,Arbing, M.,Guo, F.,Cascio, D.,Eisenberg, D.
Structure and Proposed Activity of a Member of the VapBC Family of Toxin-Antitoxin Systems: VapBC-5 FROM MYCOBACTERIUM TUBERCULOSIS.
J.Biol.Chem., 284:276-283, 2009

PubMed Abstract: In prokaryotes, cognate toxin-antitoxin pairs have long been known, but no three-dimensional structure has been available for any given complex from Mycobacterium tuberculosis. Here we report the crystal structure and activity of a member of the VapBC family of complexes from M. tuberculosis. The toxin VapC-5 is a compact, 150 residues, two domain alpha/beta protein. Bent around the toxin is the VapB-5 antitoxin, a 33-residue alpha-helix. Assays suggest that the toxin is an Mg-enabled endoribonuclease, inhibited by the antitoxin. The lack of DNase activity is consistent with earlier suggestions that the complex represses its own operon. Furthermore, analysis of the interactions in the binding of the antitoxin to the toxin suggest that exquisite control is required to protect the bacteria cell from toxic VapC-5.

PubMed: 18952600
DOI: 10.1074/jbc.M805061200

実験手法

X-RAY DIFFRACTION (1.76 Å)