PDBsum entry 2v8o

Hydrolase

PDB id: 2v8o

Contents

Protein chain

429 a.a. *

Waters ×284

* Residue conservation analysis

PDB id:

2v8o

Name:

Hydrolase

Title:

Structure of the murray valley encephalitis virus RNA helicase to 1. 9a resolution

Structure:

Flavivirin protease ns3. Chain: a. Fragment: ns3 helicase domain, residues 1681-2122. Synonym: ns3 helicase. Engineered: yes

Source:

Murray valley encephalitis virus. Organism_taxid: 11079. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008. Expression_system_variant: rosetta plyss

Resolution:

1.90Å R-factor: 0.182 R-free: 0.223

Authors:

E.J.Mancini,R.Assenberg,A.Verma,T.S.Walter,R.Tuma,J.M.Grimes, R.J.Owens,D.I.Stuart

Key ref:

E.J.Mancini et al. (2007). Structure of the Murray Valley encephalitis virus RNA helicase at 1.9 A resolution. Protein Sci, 16, 2294-2300. PubMed id: 17893366 DOI: 10.1110/ps.072843107

Date:

09-Aug-07 Release date: 21-Aug-07

Protein chain

P05769  (POLG_MVEV5) -  Genome polyprotein from Murray valley encephalitis virus (strain MVE-1-51)

Seq: 3434 a.a.

Struc: 429 a.a.*

* PDB and UniProt seqs differ at 2 residue positions (black crosses)

Enzyme reactions

• Enzyme class 1: E.C.2.1.1.56 - mRNA (guanine-N(7))-methyltransferase.
• Reaction: a 5'-end (5'-triphosphoguanosine)-ribonucleoside in mRNA + S-adenosyl-L- methionine = a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleoside in mRNA + S-adenosyl-L-homocysteine
• Enzyme class 2: E.C.2.1.1.57 - methyltransferase cap1.
• Reaction: a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleoside in mRNA + S-adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-triphosphoguanosine)- (2'-O-methyl-ribonucleoside) in mRNA + S-adenosyl-L-homocysteine + H⁺
• Enzyme class 3: E.C.2.7.7.48 - RNA-directed Rna polymerase.
• Reaction: RNA(n) + a ribonucleoside 5'-triphosphate = RNA(n+1) + diphosphate
• Enzyme class 4: E.C.3.4.21.91 - flavivirin.
• Reaction: Selective hydrolysis of Xaa-Xaa-|-Xbb bonds in which each of the Xaa can be either Arg or Lys and Xbb can be either Ser or Ala.
• Enzyme class 5: E.C.3.6.1.15 - nucleoside-triphosphate phosphatase.
• Reaction: a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-diphosphate + phosphate + H⁺
• Enzyme class 6: E.C.3.6.4.13 - Rna helicase.
• Reaction: ATP + H2O = ADP + phosphate + H⁺

Note, where more than one E.C. class is given (as above), each may correspond to a different protein domain or, in the case of polyprotein precursors, to a different mature protein.

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

reference

DOI no: 10.1110/ps.072843107

Protein Sci 16:2294-2300 (2007)

PubMed id: 17893366

Structure of the Murray Valley encephalitis virus RNA helicase at 1.9 A resolution.

E.J.Mancini, R.Assenberg, A.Verma, T.S.Walter, R.Tuma, J.M.Grimes, R.J.Owens, D.I.Stuart.

ABSTRACT

Murray Valley encephalitis virus (MVEV), a mosquito-borne flavivirus endemic to Australia, is closely related to Japanese encephalitis virus and West Nile virus. Nonstructural protein 3 (NS3) is a multifunctional enzyme with serine protease and DEXH/D-box helicase domains, whose activity is central to flavivirus replication and is therefore a possible target for anti-flaviviral compounds. Cloning, purification, and crystal structure determination to 1.9 A resolution of the NS3 helicase of MVEV and characterization of its enzymatic activity is reported. Comparison with the structures of helicases from related viruses supports a possible mechanism of ATP hydrolysis-driven strand separation.

Selected figure(s)

Figure 2.
Figure 2. (A) The structures of MVEVh (yellow) and YFVh (blue) superimposed via domain 3 (superimposition performed using

The above figure is reprinted by permission from the Protein Society: Protein Sci (2007, 16, 2294-2300) copyright 2007.

Figure was selected by an automated process.