This family of domains contain a P-loop motif that is characteristic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins.
Helicase nonstructural protein 13 (NSP13) is encoded by the replicase polyprotein 1a/ab of coronaviruses and released after a proteolytic process. It plays a critical role catalysing the unwinding of duplex oligonucleotides into single strands in an ...
Helicase nonstructural protein 13 (NSP13) is encoded by the replicase polyprotein 1a/ab of coronaviruses and released after a proteolytic process. It plays a critical role catalysing the unwinding of duplex oligonucleotides into single strands in an NTP-dependent manner. It is a multidomain protein consisting of a N-terminal zinc-binding domain (ZBD), a stalk domain that connects the ZBD with the 1B domain and the helicase domain (that contains two RecA1 and RecA2 domains). ZBD, stalk and 1B domains are unique to nidovirus helicases [1]. NSP13 adopts a triangular pyramid shape in which the two RecA1 and A2 and 1B domains form the triangular base while N-terminal ZBD and stalk domains are arranged at the apex of the pyramid [1,2]. Recently, it has been reported that SARS-CoV-2 NSP13 as an interferon antagonist [3]. This is 1B domain of NSP13 [1], which has a regulatory role modulating the nucleic acid substrate binding [2].
Coronavirus Non-structural protein 13, zinc-binding domain
Helicase nonstructural protein 13 (NSP13) is encoded by the replicase polyprotein 1a/ab of coronaviruses and released after a proteolytic process. It plays a critical role catalysing the unwinding of duplex oligonucleotides into single strands in an ...
Helicase nonstructural protein 13 (NSP13) is encoded by the replicase polyprotein 1a/ab of coronaviruses and released after a proteolytic process. It plays a critical role catalysing the unwinding of duplex oligonucleotides into single strands in an NTP-dependent manner. It In SARS-CoV, it has been shown that NSP12 directly interacts with NSP13 and enhances its helicase activity. It is a multidomain protein consisting of a N-terminal zinc-binding domain (ZBD), a stalk domain that connects the ZBD with the 1B domain and the helicase domain (that contains two RecA1 and RecA2 domains). ZBD, stalk and 1B domains are unique to nidovirus helicases [1]. NSP13 adopts a triangular pyramid shape in which the two RecA1 and A2 and 1B domains form the triangular base while N-terminal ZBD and stalk domains are arranged at the apex of the pyramid [1,2]. Recently, it has been reported that SARS-CoV-2 NSP13 as an interferon antagonist [3]. This is the zinc-binding domain (ZBD) found at the N-terminal of NSP13 which is critically involved in nidovirus replication and transcription, modulating the ATPase/helicase activity in cis [1,2]. It includes conserved cysteines and histidines involved in three zinc-binding sites [4].
Coronavirus Nonstructural protein 13, stalk domain
Helicase nonstructural protein 13 (NSP13) is encoded by the replicase polyprotein 1a/ab of coronaviruses and released after a proteolytic process. It plays a critical role catalysing the unwinding of duplex oligonucleotides into single strands in a N ...
Helicase nonstructural protein 13 (NSP13) is encoded by the replicase polyprotein 1a/ab of coronaviruses and released after a proteolytic process. It plays a critical role catalysing the unwinding of duplex oligonucleotides into single strands in a NTP-dependent manner. It is a multidomain protein consisting of a N-terminal zinc-binding domain (ZBD), a stalk domain that connects the ZBD with the 1B domain and the helicase domain (that contains two RecA1 and RecA2 domains). The ZBD, stalk and 1B domains are unique to nidovirus helicases [1]. NSP13 adopts a triangular pyramid shape in which the two RecA1 and A2 and 1B domains form the triangular base while N-terminal ZBD and stalk domains are arranged at the apex of the pyramid [1,2]. Recently, it has been reported that SARS-CoV-2 NSP13 as an interferon antagonist [3]. This is the stalk domain.
