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2etd

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

    Title Crystal structure of LEMA protein (tm0961) from THERMOTOGA MARITIMA at 2.28 A resolution. To be published
    Site JCSG
    PDB Id 2etd Target Id
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    Molecular Characteristics
    Source
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    Alias Ids
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    TPS1396,TM0961, PF04011
    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 1
    Resolution (Å)
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    Rfree
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    Matthews' coefficent 2.29 Rfactor 0.216
    Waters
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    Solvent Content 46.39

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    Ligand Information
    Ligands
    Metals

    Jmol

     
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    Google Scholar output for 2etd
    1. Decision-making in structure solution using Bayesian estimates of map quality: the PHENIX AutoSol wizard
    TC Terwilliger, PD Adams, RJ Read - Section D: Biological , 2009 - scripts.iucr.org
     
    2. Automatic procedure for using models of proteins in molecular replacement
    D Raimondo, A Giorgetti, S Bosi - PROTEINS: Structure, , 2007 - Wiley Online Library
     
    3. Structure and ligand binding of the soluble domain of a Thermotoga maritima membrane protein of unknown function TM1634
    CJ McCleverty, L Columbus, A Kreusch - Protein , 2008 - Wiley Online Library
     

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    Protein Summary

    The gene TM0961 from Thermotoga maritima encodes a predicted transmembrane protein (NP_228769) from the LemA family PF04011.

    SCOP classifies 2etd in the all alpha class, bromodomain-like fold, LemA-like (super)family. DALI weak hits are with the huntingtin interacting protein-12

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    (Z=9), pectin methylesterase inhibitor
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    (Z=9) and the uncharacterized XCC0516 protein
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    (Z=9).

    The protein is highly conserved among different bacterial species.  The LemA protein family performs regulatory functions. In the context of bacterial intracellular pathogens, they modulate guest-host relationships.  For example, the LemA gene is required for pathogenicity of Pseudomonas syringae on bean [Ref].  The LemA proteins contain a transmembrane domain and an N-terminal extracellular domain.  The exposed N-terminal domain of the LemA protein is the major antigen for recognition by the immune system of the infected multicellular organism [Ref].    

    Ligand Summary



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