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1o0x

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

    Title Crystal structure of a methionine aminopeptidase (TM1478) from Thermotoga maritima at 1.9 A resolution. Proteins 56 396-400 2004
    Site JCSG
    PDB Id 1o0x Target Id 283335
    Molecular Characteristics
    Source Thermotoga maritima msb8
    Alias Ids TPS1292,TM1478, 84823, 84817 Molecular Weight 27487.50 Da.
    Residues 250 Isoelectric Point 6.62
    Sequence miriktpseiekmkkagkavavalrevrkvivpgktawdvetlvleifkklrvkpafkgyggykyatcv svneevvhglplkekvfkegdivsvdvgavyqglygdaavtyivgetdergkelvrvtrevlekaikmi kpgirlgdvshciqetvesvgfnvirdyvghgvgrelhedpqipnygtpgtgvvlrkgmtlaiepmvse gdwrvvvkedgwtavtvdgsrcahfehtilitengaeiltkeg
      BLAST   FFAS

    Structure Determination
    Method XRAY Chains 1
    Resolution (Å) 1.90 Rfree 0.254
    Matthews' coefficent 2.47 Rfactor 0.203
    Waters 195 Solvent Content 50.14

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    Ligand Information
    Ligands
    Metals

    Jmol

     
    Google Scholar output for 1o0x
    1. Assessment of homology_based predictions in CASP5
    A Tramontano, V Morea - Proteins: Structure, Function, and , 2003 - Wiley Online Library
     
    2. Microbial biochemistry, physiology, and biotechnology of hyperthermophilic Thermotoga species
    SB Conners, EF Mongodin, MR Johnson - FEMS microbiology , 2006 - Wiley Online Library
     
    3. Evaluating the usefulness of protein structure models for molecular replacement
    A Giorgetti, D Raimondo, AE Miele - Bioinformatics, 2005 - Oxford Univ Press
     
    4. Using property based sequence motifs and 3D modeling to determine structure and functional regions of proteins
    I Ovidiu, O Numan, VS Mathura - Current medicinal , 2004 - ingentaconnect.com
     
    5. CASP5 target classification
    LN Kinch, Y Qi, TJP Hubbard - : Structure, Function, and , 2003 - Wiley Online Library
     
    6. Automatic procedure for using models of proteins in molecular replacement
    D Raimondo, A Giorgetti, S Bosi - PROTEINS: Structure, , 2007 - Wiley Online Library
     
    7. Crystal structure of a methionine aminopeptidase (TM1478) from Thermotoga maritima at 1.9 resolution
    G Spraggon, R Schwarzenbacher - Proteins: Structure, , 2004 - Wiley Online Library
     
    8. A fold-recognition approach to loop modeling
    C Levefelt, D Lundh - Journal of molecular modeling, 2006 - Springer
     
    9. A seqlet-based maximum entropy Markov approach for protein secondary structure prediction
    Q Dong, X Wang, L Lin, Y Guan - Science in China Series C: Life Sciences, 2005 - Springer
     
    10. Structure_based identification of catalytic residues
    R Yahalom, D Reshef, A Wiener - Proteins: Structure, , 2011 - Wiley Online Library
     
    11. A fourier fingerprint-based method for protein surface representation
    MJ Bayley, EJ Gardiner, P Willett - Journal of chemical , 2005 - ACS Publications
     
    12. Protein Structure Prediction Using an Augmented Homology Modeling Method: Key Importance of Iterative-Procedures for Obtaining Consistent Quality Models
    S McDonald, S Mylvaganam - Current , 2005 - ingentaconnect.com
     
    13. Of sequence and structure: Strategies of protein thermostability in evolutionary perspective
    IN Berezovsky, EI Shakhnovich - Arxiv preprint q-bio/0408007, 2004 - arxiv.org
     
    14. Carbohydrate utilization pathway analysis in the hyperthermophile Thermotoga maritima
    SB Conners - 2006 - repository.lib.ncsu.edu
     
    15. Predicting protein interaction interfaces from protein sequences: Case studies of subtilisin and phycocyanin
    BB Xie, XL Chen, XY Zhang, HL He - Proteins: Structure, , 2008 - Wiley Online Library
     
    16. Fragment Library-Based Representation System for Protein Conformation
    R Kim, CY Choi - Protein and Peptide Letters, 2006 - ingentaconnect.com
     

    Protein Summary

    The TM1478 gene of Thermotoga maritima encodes a methionine aminopeptidase (MAP; EC 3.4.11.18, PubMed:15211524, cd01086), that removes the ubiquitous N-terminal methionine from nascent proteins.  Methionine aminopeptidases are target proteins for the development of both anticancer and antibacterial compounds (PubMed:16420038).

    Protein encoded by TM1478 has creatinase/aminopeptidase fold (SCOP sunid:55919) with duplication composed of two very similar alpha+beta folds.


    Ligand Summary



    References

    Reviews

    References

     

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