1SH2

Crystal Structure of Norwalk Virus Polymerase (Metal-free, Centered Orthorhombic)

Summary for 1SH2

• Entry DOI: 10.2210/pdb1sh2/pdb
• Related: 1KHV 1SH0 1SH3
• Descriptor: RNA Polymerase (2 entities in total)
• Functional Keywords: rna polymerase, viral enzyme, viral replication, transferase
• Biological source: Norwalk virus
• Total number of polymer chains: 1
• Total formula weight: 56813.55

Authors

Ng, K.K.,Pendas-Franco, N.,Rojo, J.,Boga, J.A.,Machin, A.,Alonso, J.M.,Parra, F. (deposition date: 2004-02-24, release date: 2004-03-09, Last modification date: 2023-08-23)

Primary citation

Ng, K.K.,Pendas-Franco, N.,Rojo, J.,Boga, J.A.,Machin, A.,Alonso, J.M.,Parra, F.
Crystal structure of norwalk virus polymerase reveals the carboxyl terminus in the active site cleft.
J.Biol.Chem., 279:16638-16645, 2004

PubMed Abstract: Norwalk virus is a major cause of acute gastroenteritis for which effective treatments are sorely lacking. To provide a basis for the rational design of novel antiviral agents, the main replication enzyme in Norwalk virus, the virally encoded RNA-dependent RNA polymerase (RdRP), has been expressed in an enzymatically active form, and its structure has been crystallographically determined both in the presence and absence of divalent metal cations. Although the overall fold of the enzyme is similar to that seen previously in the RdRP from rabbit hemorrhagic disease virus, the carboxyl terminus, surprisingly, is located in the active site cleft in five independent copies of the protein in three distinct crystal forms. The location of this carboxyl-terminal segment appears to interfere with the binding of double-stranded RNA in the active site cleft and may play a role in the initiation of RNA synthesis or mediate interactions with accessory replication proteins.

PubMed: 14764591
DOI: 10.1074/jbc.M400584200

Experimental method

X-RAY DIFFRACTION (2.3 Å)