4EHC

Crystal structure of the C-terminal domain of Rv0977 of Mycobacterium tuberculosis

4EHC の概要

• エントリーDOI: 10.2210/pdb4ehc/pdb
• 分子名称: PE-PGRS FAMILY PROTEIN, ZINC ION, 1,2-ETHANEDIOL, ... (4 entities in total)
• 機能のキーワード: aspartic proteinase, hydrolase
• 由来する生物種: Mycobacterium tuberculosis
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 32271.06

構造登録者

Barathy, D.V.,Suguna, K. (登録日: 2012-04-02, 公開日: 2013-06-19, 最終更新日: 2024-10-09)

主引用文献

Barathy, D.V.,Suguna, K.
Crystal structure of a putative aspartic proteinase domain of the Mycobacterium tuberculosis cell surface antigen PE_PGRS16
FEBS Open Bio, 3:256-262, 2013

PubMed Abstract: We report the crystal structure of the first prokaryotic aspartic proteinase-like domain identified in the genome of Mycobacterium tuberculosis. A search in the genomes of Mycobacterium species showed that the C-terminal domains of some of the PE family proteins contain two classic DT/SG motifs of aspartic proteinases with a low overall sequence similarity to HIV proteinase. The three-dimensional structure of one of them, Rv0977 (PE_PGRS16) of M. tuberculosis revealed the characteristic pepsin-fold and catalytic site architecture. However, the active site was completely blocked by the N-terminal His-tag. Surprisingly, the enzyme was found to be inactive even after the removal of the N-terminal His-tag. A comparison of the structure with pepsins showed significant differences in the critical substrate binding residues and in the flap tyrosine conformation that could contribute to the lack of proteolytic activity of Rv0977.

PubMed: 23923105
DOI: 10.1016/j.fob.2013.05.004

実験手法

X-RAY DIFFRACTION (1.98 Å)