The Open Protein Structure Annotation Network
PDB Keyword


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

    Title Crystal structure of (tm1088a) from THERMOTOGA MARITIMA at 1.50 A resolution. To be published
    Site JCSG
    PDB Id 2g1u Target Id 358957
    Molecular Characteristics
    Source Thermotoga maritima msb8
    Alias Ids TPS1408,TM1088A Molecular Weight 16032.54 Da.
    Residues 143 Isoelectric Point 5.12
    Sequence mskkqkskyivifgcgrlgslianlasssghsvvvvdkneyafhrlnsefsgftvvgdaaefetlkecg mekadmvfaftnddstnffismnarymfnvenviarvydpekikifeengikticpavlmiekvkefii gseed
      BLAST   FFAS

    Structure Determination
    Method XRAY Chains 1
    Resolution (Å) 1.50 Rfree 0.175
    Matthews' coefficent 2.44 Rfactor 0.153
    Waters 110 Solvent Content 49.14

    Ligand Information


    Google Scholar output for 2g1u
    1. The JCSG MR pipeline: optimized alignments, multiple models and parallel searches
    R Schwarzenbacher, A Godzik - Section D: Biological , 2007 - scripts.iucr.org
    2. Comprehensive structural classification of ligand-binding motifs in proteins
    AR Kinjo, H Nakamura - Structure, 2009 - Elsevier
    3. Mechanism of ligand-gated potassium efflux in bacterial pathogens
    TP Roosild, S Castronovo, J Healy - Proceedings of the , 2010 - National Acad Sciences
    4. The Thermotoga maritima Trk Potassium Transporterfrom Frameshift to Function
    HA Johnson, E Hampton, SA Lesley - Journal of bacteriology, 2009 - Am Soc Microbiol

    Protein Summary

    The gene TM1088A from Thermotoga maritima encodes an N-terminal domain from TrkA protein (KTN) PF02254.  The protein belongs to the class of alpha and beta (a+b) proteins and adopts a NAD(P)-binding Rossmann-domain fold type SCOP51734.  KTN domain is a highly conserved cytoplasmic domain present ubiquitously in a variety of prokaryotic and eukaryotic K+ channels and transporters.  KTN domain plays a central role in the regulation and coordination of K+ flux across cellular membranes.  KTN domain forms tetramers in the solution  in a ligand-dependent ( NAD+ and NADH) manner 1LSS [Ref]. These ligands are essential for maintenance of the tetrameric state of KTN in solution.  Maintenance of cytoplasmic potassium levels is a vital homeostatic function, critical for cell growth and survival.   Bacterial K+ transport systems are of medicinal interest, as they play central roles in the survival of pathogenic microbes in hostile host environments.

    Ligand Summary





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