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2fup

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

    Title Crystal structure of hypothetical protein (NP_252042.1) from Pseudomonas aeruginosa at 1.48 A resolution. To be published
    Site JCSG
    PDB Id 2fup Target Id 369551
    Molecular Characteristics
    Source Pseudomonas aeruginosa pao1
    Alias Ids TPS1547,NP_252042.1, 85225 Molecular Weight 17254.38 Da.
    Residues 156 Isoelectric Point 5.31
    Sequence mpdsptlldlfaedighanqllqlvdeefqalerrelpvlqqllgakqplmqqlerngraraeilreag vsldreglaryareradgaellargdelgellercqqanlrngriiranqastgsllnilrgqdapsly dsrggtasssrqrplsqa
      BLAST   FFAS

    Structure Determination
    Method XRAY Chains 1
    Resolution (Å) 1.48 Rfree 0.218
    Matthews' coefficent 2.25 Rfactor 0.188
    Waters 110 Solvent Content 45.32

    Ligand Information
    Ligands
    Metals

    Jmol

     
    Google Scholar output for 2fup
    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. Structural insight into the regulatory mechanisms of interactions of the flagellar type III chaperone FliT with its binding partners
    K Imada, T Minamino, M Kinoshita - Proceedings of the , 2010 - National Acad Sciences
     
    3. Evidence for a coiled-coil interaction mode of disordered proteins from bacterial type III secretion systems
    AD Gazi, M Bastaki, SN Charova - Journal of Biological , 2008 - ASBMB
     
    4. Interaction of a bacterial flagellar chaperone FlgN with FlhA is required for efficient export of its cognate substrates
    T Minamino, M Kinoshita, N Hara - Molecular , 2012 - Wiley Online Library
     
    5. Structural Insights on Two Hypothetical Secretion Chaperones from Xanthomonas axonopodis pv. citri
    J Fattori, A Prando, LHP Assis, R Aparicio, L Tasic - The Protein Journal, 2011 - Springer
     
    6. Common architecture between the flagellar type III ATPase complex and F1-ATPase revealed by the structure of FliJ
    T Ibuki - 2010 - ir.library.osaka-u.ac.jp
     
    7. A Machine Learning Approach for the Identification of Protein Secondary Structure Elements from Electron Cryo_Microscopy Density Maps
    D Si, S Ji, KA Nasr, J He - Biopolymers, 2012 - Wiley Online Library
     

    Protein Summary

    The gene PA3352 from Pseudomonas aeruginosa encodes the NP_252042 protein that belongs to the FlgN-like group PF05130. Analysis of its genome context indicates a possible functional link (score 0.66) with the fagellar basal body P-ring biosynthesis protein PA3350.

    The 2fup structure belongs to the class of all alpha proteins and adopts a STAT-like fold type SCOP47654 inside the FlgN-like (super)family. DALI top hits are with the transcription factors STAT3B 1bg1 and 1y1u (Z=10) followed by the SSO1 protein 1fio (Z=10). 

    FlgN-like proteins are structurally related to type III secretion chaperones [Ref].  The function of FlgN is to facilitate the initiation of flagella filament assembly, a role that may be critical in attaining the much higher concentration of surface flagellin required for swarming.  It has been shown in vitro that FlgN specifically binds to flagellar proteins [Ref]. The flagellar axial proteins destined for polymerization into the cell surface structure are exported through the 25–30 A ̊flagellum central channel as partially unfolded monomers.  Thus, most probably FlgN functions as export chaperone [Ref].

    Ligand Summary


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