1N35

lambda3 elongation complex with four phosphodiester bond formed


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.50 Å
  • R-Value Free: 0.259 
  • R-Value Work: 0.207 
  • R-Value Observed: 0.207 

Starting Model: experimental
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This is version 1.4 of the entry. See complete history


Literature

RNA Synthesis in a Cage--Structural Studies of Reovirus Polymerase [lambda] 3

Tao, Y.Farsetta, D.L.Nibert, M.L.Harrison, S.C.

(2002) Cell 111: 733-745

  • DOI: https://doi.org/10.1016/s0092-8674(02)01110-8
  • Primary Citation of Related Structures:  
    1MUK, 1MWH, 1N1H, 1N35, 1N38

  • PubMed Abstract: 

    The reovirus polymerase and those of other dsRNA viruses function within the confines of a protein capsid to transcribe the tightly packed dsRNA genome segments. The crystal structure of the reovirus polymerase, lambda3, determined at 2.5 A resolution, shows a fingers-palm-thumb core, similar to those of other viral polymerases, surrounded by major N- and C-terminal elaborations, which create a cage-like structure, with four channels leading to the catalytic site. This "caged" polymerase has allowed us to visualize the results of several rounds of RNA polymerization directly in the crystals. A 5' cap binding site on the surface of lambda3 suggests a template retention mechanism by which attachment of the 5' end of the plus-sense strand facilitates insertion of the 3' end of the minus-sense strand into the template channel.


  • Organizational Affiliation

    Howard Hughes Medical Institute, Department of Molecular and Cellular Biology, Harvard University, Cambridge, MA 02138, USA.


Macromolecules

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Entity ID: 3
MoleculeChains Sequence LengthOrganismDetailsImage
Minor core protein lambda 3C [auth A]1,267Mammalian orthoreovirus 3 DearingMutation(s): 0 
Gene Names: L1
EC: 2.7.7.48
UniProt
Find proteins for P0CK31 (Reovirus type 3 (strain Dearing))
Explore P0CK31 
Go to UniProtKB:  P0CK31
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP0CK31
Sequence Annotations
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  • Reference Sequence

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Entity ID: 1
MoleculeChains LengthOrganismImage
5'-R(P*GP*GP*GP*GP*G)-3'A [auth B]5N/A
Sequence Annotations
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  • Reference Sequence

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Entity ID: 2
MoleculeChains LengthOrganismImage
5'-R(*AP*UP*UP*AP*GP*CP*CP*CP*CP*C)-3'B [auth C]10N/A
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.50 Å
  • R-Value Free: 0.259 
  • R-Value Work: 0.207 
  • R-Value Observed: 0.207 
  • Space Group: P 21 21 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 70.883α = 90
b = 85.013β = 90
c = 249.294γ = 90
Software Package:
Software NamePurpose
DENZOdata reduction
SCALEPACKdata scaling
CNSrefinement
CNSphasing

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2002-12-25
    Type: Initial release
  • Version 1.1: 2008-04-28
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2024-02-14
    Changes: Data collection, Database references, Derived calculations
  • Version 1.4: 2024-04-03
    Changes: Refinement description