Selected article for: "activity low adrp pase adp phosphatase and adp phosphatase"
Author: Tan, Jinzhi; Vonrhein, Clemens; Smart, Oliver S.; Bricogne, Gerard; Bollati, Michela; Kusov, Yuri; Hansen, Guido; Mesters, Jeroen R.; Schmidt, Christian L.; Hilgenfeld, Rolf
Title: The SARS-Unique Domain (SUD) of SARS Coronavirus Contains Two Macrodomains That Bind G-Quadruplexes
  • Document date: 2009_5_15
    • ID: 1aqt65cc_26
    Snippet: Our identification of two macrodomains in SUD core brings the number of these domains in SARS-CoV Nsp3 to three. What are the functions of these modules? The original SARS-CoV ''Xdomain'' (Nsp3b) has been shown to have low ADP-ribose-10phosphate phosphatase (Appr-10-pase or ''ADRP'') activity [21] [22] [23] . However, this assignment is controversial. A nuclear Appr-10pase (Poa1p in yeast, [20] ) is an enzyme of a tRNA metabolic pathway, but ther.....
    Document: Our identification of two macrodomains in SUD core brings the number of these domains in SARS-CoV Nsp3 to three. What are the functions of these modules? The original SARS-CoV ''Xdomain'' (Nsp3b) has been shown to have low ADP-ribose-10phosphate phosphatase (Appr-10-pase or ''ADRP'') activity [21] [22] [23] . However, this assignment is controversial. A nuclear Appr-10pase (Poa1p in yeast, [20] ) is an enzyme of a tRNA metabolic pathway, but there is no evidence for coronavirus Nsp3 ever being translocated to the nucleus, and the other enzymes involved in this pathway are missing in coronaviruses (with the exception of the cyclic 10,20-phosphodiesterase (CPDase) in group 2a viruses such as Mouse Hepatitis Virus, Bovine Coronavirus, and Human Coronavirus OC43). Therefore, it has been proposed that the Xdomain may be involved in binding poly(ADP-ribose), a metabolic product of NAD + synthesized by the enzyme poly(ADP-ribose) polymerase (PARP; [23] ). However, we have recently demonstrated that the X-domain of Infectious Bronchitis Virus (IBV) strain Beaudette, a group-3 coronavirus, does not have significant affinity to ADP-ribose [24] . This can be explained on the basis of crystal structures: In the X-domain (Nsp3b) of SARS-CoV [23] , and in that of HCoV 229E [24] , a stretch of three conserved glycine residues is involved in binding the pyrophosphate unit of ADP-ribose, whereas in the corresponding domain of IBV strain Beaudette (but not in all IBV strains, see [44] ), the second glycine is replaced by serine, leading to steric interference with ADPribose binding [24] . In the two SUD subdomains, the tripleglycine sequence is not conserved (see Figure 2C ), and hence, they do not bind ADP-ribose either.

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