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The Open Protein Structure Annotation Network
PDB Keyword
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1lme

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

    Title Structure analysis of peptide deformylases from streptococcus pneumoniae,staphylococcus aureus, thermotoga maritima, and pseudomonas aeruginosa: snapshots of the oxygen sensitivity of peptide deformylase. J.MOL.BIOL. 330 309-321 2003
    Site JCSG
    PDB Id 1lme Target Id
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    Molecular Characteristics
    Source
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    Alias Ids
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    TPS1309,TM1661, 85072
    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 2
    Resolution (Å)
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    Rfree
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    Matthews' coefficent 2.25 Rfactor 0.198
    Waters
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    Solvent Content 45.26

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    Ligand Information
    Ligands
    Metals

    Jmol

     
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    Google Scholar output for 1lme
    1. Structure analysis of peptide deformylases from Streptococcus pneumoniae, Staphylococcus aureus, Thermotoga maritima and Pseudomonas aeruginosa: snapshots
    A Kreusch, G Spraggon, CC Lee, H Klock - Journal of molecular , 2003 - Elsevier
     
    2. Crystal structure of peptide deformylase from Staphylococcus aureus in complex with actinonin, a naturally occurring antibacterial agent
    HJ Yoon, HL Kim, SK Lee, HW Kim - Proteins: Structure, , 2004 - Wiley Online Library
     
    3. Structure analysis of peptide deformylase from Bacillus cereus
    JH Moon, JK Park, EEK Kim - Proteins: Structure, Function, and , 2005 - Wiley Online Library
     
    4. Crystallization and preliminary X-ray crystallographic analysis of peptide deformylase (PDF) from Bacillus cereus in ligand-free and actinonin-bound forms
    JK Park, JH Moon, JH Kim, EE Kim - Acta Crystallographica Section , 2004 - scripts.iucr.org
     
    5. Crystallization and preliminary X-ray crystallographic analysis of peptide deformylase from Thermus thermophilus HB8
    M Kamo, N Kudo, WC Lee, H Motoshima - Section D: Biological , 2004 - scripts.iucr.org
     

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    Protein Summary

    The gene TM1661 from Thermotoga maritima encodes  polypeptide or peptide deformylase PF01327 E.C.3.5.1.88.  The protein belongs to the class of alpha and beta (a+b) proteins and reveals peptide deformylase fold type SCOP56419.  The enzyme belongs to a family of metalloenzymes that catalyzes the removal of the N-terminal formyl group in a growing polypeptide chain following translation initiation during protein synthesis in prokaryotes.  These enzymes utilize Fe(II) as the catalytic metal ion, which can be replaced with a nickel or cobalt ion with no loss of activity. There are two types of peptide deformylases, types I and II, which differ in structure only in the outer surface of the domain. Because these enzymes are essential only in prokaryotes (although eukaryotic gene sequences have been found), they are a target for a new class of antibacterial agents [Ref].  The crystal structure of homologous enzyme from Plasmodium falciparum (malaria parasite) in complex with peptide-like inhibitor has been reported 1RL4

    Ligand Summary



    References

    Reviews

    References

     

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