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The Open Protein Structure Annotation Network
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2f1l

    Table of contents
    1. 1. Protein Summary
    2. 2. Ligand Summary
    3. 3. References

    Title Crystal structure of 16S rRNA processing protein from Pseudomonas aeruginosa at 2.46 A resolution. To be published
    Site JCSG
    PDB Id 2f1l Target Id
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    Molecular Characteristics
    Source
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    Alias Ids
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    TPS1379,NP_252433.1, 289764
    Molecular Weight
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    Da.
    Residues
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    Isoelectric Point
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    Sequence
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      BLAST   FFAS

    Structure Determination
    Method XRAY
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    Chains 1
    Resolution (Å)
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    Rfree
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    Matthews' coefficent 3.41 Rfactor 0.175
    Waters
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    Solvent Content 63.68

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    Ligand Information
    Ligands
    Metals

    Jmol

     
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    Google Scholar output for 2f1l
    1. Cradle-loop barrels and the concept of metafolds in protein classification by natural descent
    V Alva, KK Koretke, M Coles, AN Lupas - Current opinion in structural , 2008 - Elsevier
     
    2. Structural characterization of the ribosome maturation protein, RimM
    S Suzuki, A Tatsuguchi, E Matsumoto - Journal of , 2007 - Am Soc Microbiol
     

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    Protein Summary

    The gene PA3744 from Pseudomonas aeruginosa encodes the NP_252433 protein with two domains: a putative 16S rRNA processing protein belonging to the RimM (N-terminal domain) group (PF01782); and a PRC barrel C-terminal domain found in the RNA metabolism proteins of the RimM group (PF05239). STRING analysis indicates a functional link (score 0.99) of PA3744 with its genomic neighbor trmD, a tRNA-methyltransferase.

    The 2f1l N-terminal domain structure adopts a reductase/isomerase/elongation factor comon domain fold, inside the RimM N-terminal domain family; the C-terminal domain shows a PRC barrel domain fold, inside the RimM C-terminal domain family. The structures of homologous proteins  from other organisms have been determined: 3H9N (Dali Zscr=14), from Haemophilus influenzae; 2DOG (Z=13), from Thermus thermophilus HB8.

    Within the context of a 16S rRNA processing protein, this C-terminal domain might be involved in hydrophilic substrate (RNA) binding.  

    Ligand Summary



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