The Open Protein Structure Annotation Network
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    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

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    Ligand Information


    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





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