4HEC

Crystal structure of a putative uncharacterized protein from Mycobacterium tuberculosis

4HEC の概要

• エントリーDOI: 10.2210/pdb4hec/pdb
• 分子名称: Putative uncharacterized protein, MAGNESIUM ION (3 entities in total)
• 機能のキーワード: ssgcid, mycobacterium tuberculosis, structural genomics, seattle structural genomics center for infectious disease, unknown function
• 由来する生物種: Mycobacterium tuberculosis
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 43918.03

構造登録者

Seattle Structural Genomics Center for Infectious Disease (SSGCID) (登録日: 2012-10-03, 公開日: 2012-10-17, 最終更新日: 2024-04-03)

主引用文献

Abendroth, J.,Ollodart, A.,Andrews, E.S.,Myler, P.J.,Staker, B.L.,Edwards, T.E.,Arcus, V.L.,Grundner, C.
Mycobacterium tuberculosis Rv2179c Protein Establishes a New Exoribonuclease Family with Broad Phylogenetic Distribution.
J.Biol.Chem., 289:2139-2147, 2014

PubMed Abstract: Ribonucleases (RNases) maintain the cellular RNA pool by RNA processing and degradation. In many bacteria, including the human pathogen Mycobacterium tuberculosis (Mtb), the enzymes mediating several central RNA processing functions are still unknown. Here, we identify the hypothetical Mtb protein Rv2179c as a highly divergent exoribonuclease. Although the primary sequence of Rv2179c has no detectable similarity to any known RNase, the Rv2179c crystal structure reveals an RNase fold. Active site residues are equivalent to those in the DEDD family of RNases, and Rv2179c has close structural homology to Escherichia coli RNase T. Consistent with the DEDD fold, Rv2179c has exoribonuclease activity, cleaving the 3' single-strand overhangs of duplex RNA. Functional orthologs of Rv2179c are prevalent in actinobacteria and found in bacteria as phylogenetically distant as proteobacteria. Thus, Rv2179c is the founding member of a new, large RNase family with hundreds of members across the bacterial kingdom.

PubMed: 24311791
DOI: 10.1074/jbc.M113.525683

実験手法

X-RAY DIFFRACTION (1.8 Å)