Abstract
Viral genome replication in Flaviviridae is carried out by a virally encoded RNA-dependent RNA polymerase (RdRp). These viruses initiate the RNA synthesis via a de novo mechanism that differs from the primer-dependent mechanism used by Picornaviridae. Like all polymerases, the structure of Flaviviridae RdRps resembles a right hand with characteristic fingers, palm, and thumb domains. Structural features that distinguish Flaviviridae RdRps from other polymerases are a large thumb domain and a C-terminal motif that encircles the active site. This domain arrangement restricts the volume of the template-binding channel, allowing only single-stranded RNA to enter the active site. While this closed form of the polymerase is ideal to stabilize a de novo initiation complex, significant conformational changes are expected to accommodate the elongation complex containing the RNA duplex product.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 746-751 |
| Number of pages | 6 |
| Journal | Current Opinion in Structural Biology |
| Volume | 19 |
| Issue number | 6 |
| DOIs | |
| State | Published - Dec 2009 |
Fingerprint
ASJC Scopus subject areas
- Molecular Biology
- Structural Biology
Cite this
RNA-dependent RNA polymerases from Flaviviridae. / Choi, Kyung; Rossmann, Michael G.
In: Current Opinion in Structural Biology, Vol. 19, No. 6, 12.2009, p. 746-751.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - RNA-dependent RNA polymerases from Flaviviridae
AU - Choi, Kyung
AU - Rossmann, Michael G.
PY - 2009/12
Y1 - 2009/12
N2 - Viral genome replication in Flaviviridae is carried out by a virally encoded RNA-dependent RNA polymerase (RdRp). These viruses initiate the RNA synthesis via a de novo mechanism that differs from the primer-dependent mechanism used by Picornaviridae. Like all polymerases, the structure of Flaviviridae RdRps resembles a right hand with characteristic fingers, palm, and thumb domains. Structural features that distinguish Flaviviridae RdRps from other polymerases are a large thumb domain and a C-terminal motif that encircles the active site. This domain arrangement restricts the volume of the template-binding channel, allowing only single-stranded RNA to enter the active site. While this closed form of the polymerase is ideal to stabilize a de novo initiation complex, significant conformational changes are expected to accommodate the elongation complex containing the RNA duplex product.
AB - Viral genome replication in Flaviviridae is carried out by a virally encoded RNA-dependent RNA polymerase (RdRp). These viruses initiate the RNA synthesis via a de novo mechanism that differs from the primer-dependent mechanism used by Picornaviridae. Like all polymerases, the structure of Flaviviridae RdRps resembles a right hand with characteristic fingers, palm, and thumb domains. Structural features that distinguish Flaviviridae RdRps from other polymerases are a large thumb domain and a C-terminal motif that encircles the active site. This domain arrangement restricts the volume of the template-binding channel, allowing only single-stranded RNA to enter the active site. While this closed form of the polymerase is ideal to stabilize a de novo initiation complex, significant conformational changes are expected to accommodate the elongation complex containing the RNA duplex product.
UR - http://www.scopus.com/inward/record.url?scp=70549094435&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=70549094435&partnerID=8YFLogxK
U2 - 10.1016/j.sbi.2009.10.015
DO - 10.1016/j.sbi.2009.10.015
M3 - Article
C2 - 19914821
AN - SCOPUS:70549094435
VL - 19
SP - 746
EP - 751
JO - Current Opinion in Structural Biology
JF - Current Opinion in Structural Biology
SN - 0959-440X
IS - 6
ER -