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Structure paper

TitleFlexibility between the Protease and Helicase Domains of the Dengue Virus Ns3 Protein Conferred by the Linker Region and its Functional Implications.
Journal, issue, pagesJ. Biol. Chem., Vol. 285, Page 18817-, Year 2010
Publish dateMay 7, 2009 (structure data deposition date)
AuthorsLuo, D. / Wei, N. / Doan, D.N. / Paradkar, P.N. / Chong, Y. / Davidson, A.D. / Kotaka, M. / Lescar, J. / Vasudevan, S.G.
External linksJ. Biol. Chem. / PubMed:20375022
MethodsX-ray diffraction
Resolution2.2 - 2.8 Å
Structure data

PDB-2whx:
A second conformation of the NS3 protease-helicase from dengue virus
Method: X-RAY DIFFRACTION / Resolution: 2.2 Å

PDB-2wzq:
Insertion Mutant E173GP174 of the NS3 protease-helicase from dengue virus
Method: X-RAY DIFFRACTION / Resolution: 2.8 Å

Chemicals

ChemComp-ADP:
ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying molecule*YM

ChemComp-MN:
Unknown entry

ChemComp-CL:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-GOL:
GLYCEROL

Source
  • dengue virus 4
  • dengue virus
KeywordsHYDROLASE / TRANSCRIPTION / ATP-BINDING / RETICULUM / NUCLEOTIDYLTRANSFERASE / MULTIFUNCTIONAL ENZYME / TRANSCRIPTION REGULATION / RIBONUCLEOPROTEIN / RNA-DIRECTED RNA POLYMERASE / RNA REPLICATION / ENVELOPE PROTEIN / VIRION / TRANSMEMBRANE / NUCLEOTIDE-BINDING / CAPSID PROTEIN / DOMAIN MOBILITY

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