Selected article for: "catalytic activity and nucleic acid"
Author: Hao, Wei; Wojdyla, Justyna Aleksandra; Zhao, Rong; Han, Ruiyun; Das, Rajat; Zlatev, Ivan; Manoharan, Muthiah; Wang, Meitian; Cui, Sheng
Title: Crystal structure of Middle East respiratory syndrome coronavirus helicase
  • Document date: 2017_6_26
    • ID: 0vxhgjss_6
    Snippet: It has been previously shown that +RNA viruses with genome larger than 7 kb encode helicases [16] [17] [18] . Helicases unwind DNA or RNA duplexes in an NTP hydrolysis dependent manner. They are classified into six superfamilies SF1-SF6 and participate in almost every aspect of nucleic acid metabolism [19] . Regardless of their functional diversity, helicases all contain core domains that hydrolyze NTPs. The enzymatic core is formed either by the.....
    Document: It has been previously shown that +RNA viruses with genome larger than 7 kb encode helicases [16] [17] [18] . Helicases unwind DNA or RNA duplexes in an NTP hydrolysis dependent manner. They are classified into six superfamilies SF1-SF6 and participate in almost every aspect of nucleic acid metabolism [19] . Regardless of their functional diversity, helicases all contain core domains that hydrolyze NTPs. The enzymatic core is formed either by the tandem RecA-like domains within the same polypeptide chain (SF1-SF2 superfamilies) or between subunits of the functional oligomer of the helicase (SF3-SF6 superfamilies) [16] . The universal features of the RecA-like domain includes a Walker A motif forming the phosphate binding loop (P-loop), a Walker B motif coordinating magnesium and an "arginine finger" engaging γ-phosphate of ATP [18, 20, 21] . In addition to the core domains, helicases also have accessory domains or inserts with various functions, such as assisting the catalytic activity or the interacting with other protein partner [16, 17, 22] .

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