3HST

N-Terminal RNASE H domain of rv2228c from mycobacterium tuberculosis as a fusion protein with maltose binding protein

3HST の概要

• エントリーDOI: 10.2210/pdb3hst/pdb
• 関連するBIRD辞書のPRD_ID: PRD_900009
• 分子名称: Maltose-binding periplasmic protein, Protein Rv2228c/MT2287, alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose, ... (6 entities in total)
• 機能のキーワード: ribonuclease h1, rv2228c n-terminal domain, mycobacterium, tuberculosis, fusion protein, maltose binding protein, hydrolase
• 由来する生物種: Escherichia coli K-12; 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 116516.60

構造登録者

Watkins, H.A.,Baker, E.N. (登録日: 2009-06-10, 公開日: 2010-04-28, 最終更新日: 2024-02-21)

主引用文献

Watkins, H.A.,Baker, E.N.
Structural and functional characterization of an RNase HI domain from the bifunctional protein Rv2228c from Mycobacterium tuberculosis.
J.Bacteriol., 192:2878-2886, 2010

PubMed Abstract: The open reading frame Rv2228c from Mycobacterium tuberculosis is predicted to encode a protein composed of two domains, each with individual functions, annotated through sequence similarity searches. The N-terminal domain is homologous with prokaryotic and eukaryotic RNase H domains and the C-terminal domain with alpha-ribazole phosphatase (CobC). The N-terminal domain of Rv2228c (Rv2228c/N) and the full-length protein were expressed as fusions with maltose binding protein (MBP). Rv2228c/N was shown to have RNase H activity with a hybrid RNA/DNA substrate as well as double-stranded RNase activity. The full-length protein was shown to have additional CobC activity. The crystal structure of the MBP-Rv2228c/N fusion protein was solved by molecular replacement and refined at 2.25-A resolution (R = 0.182; R(free) = 0.238). The protein is monomeric in solution but associates in the crystal to form a dimer. The Rv2228c/N domain has the classic RNase H fold and catalytic machinery but lacks several surface features that play important roles in the cleavage of RNA/DNA hybrids by other RNases H. The absence of either the basic protrusion of some RNases H or the hybrid binding domain of others appears to be compensated by the C-terminal CobC domain in full-length Rv2228c. The double-stranded-RNase activity of Rv2228c/N contrasts with classical RNases H and is attributed to the absence in Rv2228c/N of a key phosphate binding pocket.

PubMed: 20363939
DOI: 10.1128/JB.01615-09

実験手法

X-RAY DIFFRACTION (2.25 Å)