Structural Basis of DEAH/RHA Helicase Activity

被引:5
作者
Chen, Michael C. [1 ,2 ]
Ferre-D'Amare, Adrian R. [1 ]
机构
[1] NHLBI, Biochem & Biophys Ctr, Bldg 10, Bethesda, MD 20892 USA
[2] Univ Cambridge, Dept Chem, Cambridge CB2, England
来源
CRYSTALS | 2017年 / 7卷 / 08期
关键词
DEAH/RHA; DExH; helicase; MLE; Prp43p; DHX36; HCV NS3; VIRUS NS3 HELICASE; DEAD-BOX PROTEINS; MOLECULE IMAGING REVEALS; G-PATCH PROTEIN; RNA HELICASES; G-QUADRUPLEXES; CRYSTAL-STRUCTURE; ATP HYDROLYSIS; TRANSLOCATION; MECHANISM;
D O I
10.3390/cryst7080253
中图分类号
O7 [晶体学];
学科分类号
0702 ; 070205 ; 0703 ; 080501 ;
摘要
DEAH/RHA helicases are members of a large group of proteins collectively termed DExH-box, which also include Ski2-like and NS3/NPH-II helicases. By binding and remodeling DNA and RNA, DEAH/RHA helicases play critical roles in many cellular processes ranging from transcription and splicing to ribosome biogenesis, innate immunity and stress granule formation. While numerous crystal structures of other DExH-box proteins helicases have been reported, no structures of DEAH/RHA helicases bound to nucleic acid substrates have been available until the recent co-crystal structures of the maleless (MLE) and Prp43p bound to RNA. This review examines how these new structures provide a starting point to understand how DEAH/RHA helicases bind to, translocate on, and unwind nucleic acid substrates.
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页数:13
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