1QMI

Crystal structure of RNA 3'-terminal phosphate cyclase, an ubiquitous enzyme with unusual topology

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.80 Å
  • R-Value Free: 0.331 
  • R-Value Work: 0.244 
  • R-Value Observed: 0.244 

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This is version 1.1 of the entry. See complete history. 


Literature

Crystal Structure of RNA 3'-Terminal Phosphate Cyclase, a Ubiquitous Enzyme with Unusual Topology

Palm, G.J., Billy, E., Filipowicz, W., Wlodawer, A.

(2000) Structure 8: 13

  • DOI: https://doi.org/10.1016/s0969-2126(00)00076-9
  • Primary Citation of Related Structures:  
    1QMH, 1QMI

  • PubMed Abstract: 

    RNA cyclases are a family of RNA-modifying enzymes that are conserved in eucarya, bacteria and archaea. They catalyze the ATP-dependent conversion of the 3'-phosphate to the 2',3'-cyclic phosphodiester at the end of RNA, in a reaction involving formation of the covalent AMP-cyclase intermediate. These enzymes might be responsible for production of the cyclic phosphate RNA ends that are known to be required by many RNA ligases in both prokaryotes and eukaryotes.

    • Organizational Affiliation: 

    Program in Structural Biology, Macromolecular Crystallography Laboratory, National Cancer Institute-FCRDC, Frederick, MD 21702, USA.


Macromolecules
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(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
RNA 3'-TERMINAL PHOSPHATE CYCLASE
A, B, C, D
347Escherichia coli K-12Mutation(s): 0 
Gene Names: RTCA
EC: 6.5.1.4
UniProt
Find proteins for P46849 (Escherichia coli (strain K12))
Explore P46849 
Go to UniProtKB:  P46849
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP46849
Sequence Annotations
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  • Reference Sequence
Small Molecules
Modified Residues  1 Unique
IDChains TypeFormula2D DiagramParent
MSE
Query on MSE
A, B, C, D
L-PEPTIDE LINKINGC5 H11 N O2 SeMET
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.80 Å
  • R-Value Free: 0.331 
  • R-Value Work: 0.244 
  • R-Value Observed: 0.244 
  • Space Group: P 21 21 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 101.8α = 90
b = 126.6β = 90
c = 128.8γ = 90
Software Package:
Software NamePurpose
DENZOdata reduction
SCALEPACKdata scaling
SHELXphasing
X-PLORphasing
X-PLORrefinement

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2000-01-11
    Type: Initial release
  • Version 1.1: 2013-04-17
    Changes: Database references, Derived calculations, Other, Source and taxonomy, Structure summary, Version format compliance