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1o22

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

    Title Crystal structure of an orphan protein (TM0875) from Thermotoga maritima at 2.00-A resolution reveals a new fold. Proteins 56 607-610 2004
    Site JCSG
    PDB Id 1o22 Target Id 282744
    Molecular Characteristics
    Source Thermotoga maritima msb8
    Alias Ids TPS1242,TM0875 Molecular Weight 18578.46 Da.
    Residues 158 Isoelectric Point 4.78
    Sequence mrlmdileilyykkgkefgilekkmkeifnetgvslepvnseligriflkisvleegeevpsfaikalt pkenavdlplgdwtdlknvfveeidyldsygdmkilseknwykiyvpyssvkkknrnelveefmkyffe skgwnpgeytfsvqeidnlf
      BLAST   FFAS

    Structure Determination
    Method XRAY Chains 1
    Resolution (Å) 2.00 Rfree 0.238
    Matthews' coefficent 2.32 Rfactor 0.182
    Waters 102 Solvent Content 46.59

    Ligand Information
    Ligands
    Metals

    Jmol

     
    Google Scholar output for 1o22
    1. Progress of structural genomics initiatives: an analysis of solved target structures
    AE Todd, RL Marsden, JM Thornton - Journal of molecular , 2005 - Elsevier
     
    2. Microbial biochemistry, physiology, and biotechnology of hyperthermophilic Thermotoga species
    SB Conners, EF Mongodin, MR Johnson - FEMS microbiology , 2006 - Wiley Online Library
     
    3. Selective prediction of interaction sites in protein structures with THEMATICS
    Y Wei, J Ko, LF Murga, MJ Ondrechen - BMC bioinformatics, 2007 - biomedcentral.com
     
    4. Shotgun crystallization strategy for structural genomics II: crystallization conditions that produce high resolution structures for T. maritima proteins
    R Page, AM Deacon, SA Lesley - Journal of structural and , 2005 - Springer
     
    5. Efficient recognition of protein fold at low sequence identity by conservative application of Psi_BLAST: validation
    FJ Stevens - Journal of Molecular Recognition, 2005 - Wiley Online Library
     
    6. Analysis of chameleon sequences by energy decomposition on a pairwise per-residue basis
    S Yoon, H Jung - The protein journal, 2006 - Springer
     
    7. Crystal structure of an orphan protein (TM0875) from Thermotoga maritima at 2.00_ resolution reveals a new fold
    C Bakolitsa, R Schwarzenbacher - Proteins: Structure, , 2004 - Wiley Online Library
     
    8. Of sequence and structure: Strategies of protein thermostability in evolutionary perspective
    IN Berezovsky, EI Shakhnovich - Arxiv preprint q-bio/0408007, 2004 - arxiv.org
     
    9. Carbohydrate utilization pathway analysis in the hyperthermophile Thermotoga maritima
    SB Conners - 2006 - repository.lib.ncsu.edu
     

    Protein Summary

    The TM0875 gene of Thermotoga maritima encodes a hypothetical protein NP_228683 (PubMed:15229892) of unknown function. Analysis of TM0875 genomic context reveals the presence of MMT1 (a predicted Co/Zn/Cd cation transporter) and an inactive homolog of metal-dependent proteases. Originally classified as an ORFan protein, its homologs were found in other Thermotoga species, and it was added to PFAM as a new family PF12967 (DUF3855).

    1o22 belongs to the alpha+beta class and has a new fold (SCOP sunid:90063): beta(2)-loop-beta(2)-alpha-beta of mixed beta-sheet with order 51243 (parallel strands: 2 and 4). The dimer is most likely the biologically relevant form.

    1o22 shows weak structural similarity with the phosphoribosylformylglycinamidine synthase 1t4a (Dali Z-scr=4.6), the yggU protein (PDB structure: 1n91; with DALI Z-scr=3;  PubMed:15229892), and with the thioesterase superfamily member (PDB structure 2cy9 - found using FATCAT), even though they have very low sequence identity.

    Ligand Summary



    References

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