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The Open Protein Structure Annotation Network
PDB Keyword
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2fzt

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

    Title Crystal structure of hypothetical protein (tm0693) from THERMOTOGA MARITIMA at 2.05 A resolution. To be published
    Site JCSG
    PDB Id 2fzt Target Id
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    Related PDB Ids 2g42 
    Molecular Characteristics
    Source
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    Alias Ids
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    TPS1446,TM0693
    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 2.20 Rfactor 0.194
    Waters
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    Solvent Content 43.66

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    Ligand Information
    Ligands
    Metals

    Jmol

     
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    Google Scholar output for 2fzt
    1. Molecular replacement using ab initio polyalanine models generated with ROSETTA
    DJ Rigden, RM Keegan, MD Winn - Acta Crystallographica Section D , 2008 - scripts.iucr.org
     
    2. EDM-DEDM and protein crystal structure solution
    R Caliandro, B Carrozzini, GL Cascarano - Section D: Biological , 2009 - scripts.iucr.org
     
    3. Template_based structure prediction and classification of transcription factors in Arabidopsis thaliana
    T Lu, Y Yang, B Yao, S Liu, Y Zhou, C Zhang - Protein Science, 2012 - Wiley Online Library
     

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    Protein Summary

    The gene TM0693 from Thermotoga maritima encodes protein of unknown function DUF3214 PF11499.  Another crystal structure of the same protein is available 2G42.  The protein belongs to the class of all alpha proteins and reveals methionine synthase domain-like fold type SCOP47643 (TM0693-like family). Genome context analysis detects a 0.85 scored hit with the holo-(acyl-carrier-protein) synthase acpS (TM0692). 

    A genome-wide BLAST sequence alignment search indicated close sequence identity (33%) of the protein to a S15 RNA-binding protein TCF52B from Thermosipho africanus (THA157).  The small (30S) bacterial ribosomal subunit is composed of 16S rRNA and 21 distinct proteins. Ribosomal protein S15 binds primarily to 16S rRNA and is required for assembly of the small subunit and for intersubunit association, thus representing a key element in the assembly of a whole ribosome.  The crystal structure of S15 from Thermus thermophilus in complex with rRNA shows some structural similarity to the TM0693 protein (1DK1 [Ref]). The structure alignment reports 64 equivalent positions with an RMSD of 2.5A and 2 twists. Thus, TM0693 might encode a putative S15 rRNA-binding protein.

    Ligand Summary


    References

    Reviews

    References

     

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