5GUS

Crystal structure of ASCH domain from Zymomonas mobilis

5GUS の概要

• エントリーDOI: 10.2210/pdb5gus/pdb
• 関連するPDBエントリー: 5GUQ
• 分子名称: Helix-turn-helix domain-containing protein, 3,6,9,12,15,18,21-HEPTAOXATRICOSANE-1,23-DIOL, CHLORIDE ION, ... (5 entities in total)
• 機能のキーワード: nuclease, hydrolase
• 由来する生物種: Zymomonas mobilis subsp. mobilis (strain ATCC 10988 / DSM 424 / LMG 404 / NCIMB 8938 / NRRL B-806 / ZM1)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 35258.52

構造登録者

Ha, S.C.,Park, S.Y.,Kim, J.S. (登録日: 2016-08-31, 公開日: 2017-08-30, 最終更新日: 2024-03-20)

主引用文献

Kim, B.N.,Shin, M.,Ha, S.C.,Park, S.Y.,Seo, P.W.,Hofmann, A.,Kim, J.S.
Crystal structure of an ASCH protein from Zymomonas mobilis and its ribonuclease activity specific for single-stranded RNA.
Sci Rep, 7:12303-12303, 2017

PubMed Abstract: Activating signal cointegrator-1 homology (ASCH) domains were initially reported in human as a part of the ASC-1 transcriptional regulator, a component of a putative RNA-interacting protein complex; their presence has now been confirmed in a wide range of organisms. Here, we have determined the trigonal and monoclinic crystal structures of an ASCH domain-containing protein from Zymomonas mobilis (ZmASCH), and analyzed the structural determinants of its nucleic acid processing activity. The protein has a central β-barrel structure with several nearby α-helices. Positively charged surface patches form a cleft that runs through the pocket formed between the β-barrel and the surrounding α-helices. We further demonstrate by means of in vitro assays that ZmASCH binds nucleic acids, and degrades single-stranded RNAs in a magnesium ion-dependent manner with a cleavage preference for the phosphodiester bond between the pyrimidine and adenine nucleotides. ZmASCH also removes a nucleotide at the 5'-end. Mutagenesis studies, guided by molecular dynamics simulations, confirmed that three residues (Tyr47, Lys53, and Ser128) situated in the cleft contribute to nucleic acid-binding and RNA cleavage activities. These structural and biochemical studies imply that prokaryotic ASCH may function to control the cellular RNA amount.

PubMed: 28951575
DOI: 10.1038/s41598-017-12186-w

実験手法

X-RAY DIFFRACTION (1.951 Å)