2DKF

Crystal Structure of TTHA0252 from Thermus thermophilus HB8, a RNA Degradation Protein of the Metallo-beta-lactamase Superfamily

2DKF の概要

• エントリーDOI: 10.2210/pdb2dkf/pdb
• 関連するPDBエントリー: 2AZ4
• 分子名称: metallo-beta-lactamase superfamily protein, ZINC ION (3 entities in total)
• 機能のキーワード: beta-casp family, metallo-beta-lactamase, ribonuclease, rnase e, thermus thermophilus, structural genomics, nppsfa, national project on protein structural and functional analyses, riken structural genomics/proteomics initiative, rsgi, hydrolase
• 由来する生物種: Thermus thermophilus
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 190308.63

構造登録者

Ishikawa, I.,Nakagawa, N.,Kuramitsu, S.,Yokoyama, S.,Masui, R.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (登録日: 2006-04-10, 公開日: 2006-12-05, 最終更新日: 2024-10-23)

主引用文献

Ishikawa, H.,Nakagawa, N.,Kuramitsu, S.,Masui, R.
Crystal structure of TTHA0252 from Thermus thermophilus HB8, a RNA degradation protein of the metallo-beta-lactamase superfamily
J.Biochem.(Tokyo), 140:535-542, 2006

PubMed Abstract: In bacterial RNA metabolism, mRNA degradation is an important process for gene expression. Recently, a novel ribonuclease (RNase), belonging to the beta-CASP family within the metallo-beta-lactamase superfamily, was identified as a functional homologue of RNase E, a major component for mRNA degradation in Escherichia coli. Here, we have determined the crystal structure of TTHA0252 from Thermus thermophilus HB8, which represents the first report of the tertiary structure of a beta-CASP family protein. TTHA0252 comprises two separate domains: a metallo-beta-lactamase domain and a "clamp" domain. The active site of the enzyme is located in a cleft between the two domains, which includes two zinc ions coordinated by seven conserved residues. Although this configuration is similar to those of other beta-lactamases, TTHA0252 has one conserved His residue characteristic of the beta-CASP family as a ligand. We also detected nuclease activity of TTHA0252 against rRNAs of T. thermophilus. Our results reveal structural and functional aspects of novel RNase E-like enzymes with a beta-CASP fold.

PubMed: 16945939
DOI: 10.1093/jb/mvj183

実験手法

X-RAY DIFFRACTION (2.8 Å)