2YCB

Structure of the archaeal beta-CASP protein with N-terminal KH domains from Methanothermobacter thermautotrophicus

2YCB の概要

• エントリーDOI: 10.2210/pdb2ycb/pdb
• 分子名称: CLEAVAGE AND POLYADENYLATION SPECIFICITY FACTOR, ZINC ION, PHOSPHATE ION, ... (5 entities in total)
• 機能のキーワード: hydrolase, beta-casp, rnase, kh, metallo-beta-lactamase
• 由来する生物種: METHANOTHERMOBACTER THERMAUTOTROPHICUS
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 146766.44

構造登録者

Silva, A.P.G.,Chechik, M.,Byrne, R.T.,Waterman, D.G.,Ng, C.L.,Dodson, E.J.,Koonin, E.V.,Antson, A.A.,Smits, C. (登録日: 2011-03-13, 公開日: 2011-05-25, 最終更新日: 2023-12-20)

主引用文献

Silva, A.P.G.,Chechik, M.,Byrne, R.T.,Waterman, D.G.,Ng, C.L.,Dodson, E.J.,Koonin, E.V.,Antson, A.A.,Smits, C.
Structure and Activity of a Novel Archaeal Beta-Casp Protein with N-Terminal Kh Domains.
Structure, 19:622-, 2011

PubMed Abstract: MTH1203, a β-CASP metallo-β-lactamase family nuclease from the archaeon Methanothermobacter thermautotrophicus, was identified as a putative nuclease that might contribute to RNA processing. The crystal structure of MTH1203 reveals that, in addition to the metallo-β-lactamase nuclease and the β-CASP domains, it contains two contiguous KH domains that are unique to MTH1203 and its orthologs. RNA-binding experiments indicate that MTH1203 preferentially binds U-rich sequences with a dissociation constant in the micromolar range. In vitro nuclease activity assays demonstrated that MTH1203 is a zinc-dependent nuclease. MTH1203 is also shown to be a dimer and, significantly, this dimerization enhances the nuclease activity. Transcription termination in archaea produces mRNA transcripts with U-rich 3' ends that could be degraded by MTH1203 considering its RNA-binding specificity. We hypothesize that this nuclease degrades mRNAs of proteins targeted for degradation and so regulates archaeal RNA turnover, possibly in concert with the exosome.

PubMed: 21565697
DOI: 10.1016/J.STR.2011.03.002

実験手法

X-RAY DIFFRACTION (3.1 Å)