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The Open Protein Structure Annotation Network
PDB Keyword
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2g1u

    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
    Ligands
    Metals

    Jmol

     
    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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