2V8O

Structure of the Murray Valley encephalitis virus RNA helicase to 1. 9A resolution

PDB DOI: https://doi.org/10.2210/pdb2V8O/pdb

Classification: HYDROLASE
Organism(s): Murray Valley encephalitis virus
Expression System: Escherichia coli BL21(DE3)
Mutation(s): No

Deposited: 2007-08-09 Released: 2007-08-21
Deposition Author(s): Mancini, E.J., Assenberg, R., Verma, A., Walter, T.S., Tuma, R., Grimes, J.M., Owens, R.J., Stuart, D.I.

Experimental Data Snapshot

Method: X-RAY DIFFRACTION
Resolution: 1.90 Å
R-Value Free: 0.223
R-Value Work: 0.180
R-Value Observed: 0.182

wwPDB Validation 3D Report Full Report

This is version 1.4 of the entry. See complete history.

Literature

Structure of the Murray Valley Encephalitis Virus RNA Helicase at 1.9 A Resolution.

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

(2007) Protein Sci 16: 2294

PubMed: 17893366 Search on PubMedSearch on PubMed Central
DOI: https://doi.org/10.1110/ps.072843107
Primary Citation of Related Structures:
2V8O

PubMed 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 Angstrom 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.

Organizational Affiliation

Division of Structural Biology and Oxford Protein Production Facility, The Henry Wellcome Building for Genomic Medicine, Oxford University, Oxford, UK.

Macromolecule Content

Total Structure Weight: 49.86 kDa
Atom Count: 3,667
Modelled Residue Count: 429
Deposited Residue Count: 444
Unique protein chains: 1

Macromolecules

Find similar proteins by:

(by identity cutoff) | 3D Structure

Entity ID: 1
Molecule	Chains	Sequence Length	Organism	Details	Image
FLAVIVIRIN PROTEASE NS3	A	444	Murray Valley encephalitis virus	Mutation(s): 0 EC: 3.4.21.91
UniProt
Find proteins for P05769 (Murray valley encephalitis virus (strain MVE-1-51)) Explore P05769 Go to UniProtKB: P05769
Entity Groups
Sequence Clusters	30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt Group	P05769
Sequence Annotations Expand
Reference Sequence

Experimental Data & Validation

Experimental Data

Method: X-RAY DIFFRACTION
Resolution: 1.90 Å
R-Value Free: 0.223
R-Value Work: 0.180
R-Value Observed: 0.182
Space Group: P 1 2₁ 1

Unit Cell:

Length ( Å )	Angle ( ˚ )
a = 42.516	α = 90
b = 76.414	β = 91.73
c = 70.609	γ = 90

Software Package:

Software Name	Purpose
REFMAC	refinement
DENZO	data reduction
SCALEPACK	data scaling
CaspR	phasing

Structure Validation

View Full Validation Report

Entry History

Deposition Data

Released Date: 2007-08-21

Deposition Author(s):

Revision History (Full details and data files)

Version 1.0: 2007-08-21
Type: Initial release
Version 1.1: 2011-07-13
Changes: Advisory, Version format compliance
Version 1.2: 2017-07-12
Changes: Refinement description
Version 1.3: 2019-04-03
Changes: Data collection, Source and taxonomy
Version 1.4: 2023-12-13
Changes: Data collection, Database references, Other, Refinement description