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1ywy

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

    Title Solution Structure of Pseudomonas aeruginosa Protein PA2021. To be Published
    Site NESGC
    PDB Id 1ywy Target Id PaT85
    Molecular Characteristics
    Source Pseudomonas aeruginosa
    Alias Ids TPS9009,6736, PF11462 Molecular Weight 8216.66 Da.
    Residues 74 Isoelectric Point 4.78
    Sequence msieidseqgvcsveiegsrhrapvdslrigtdaearlsvlyidgkrlhiseedaqrlvvagaedqrrh lmadd
      BLAST   FFAS

    Structure Determination
    Method NMR Chains 1

    Ligand Information
    Ligands
    Metals

    Jmol

     
    Google Scholar output for 1ywy
    1. Bacterial pleckstrin homology domains: a prokaryotic origin for the PH domain
    Q Xu, A Bateman, RD Finn, P Abdubek - Journal of molecular , 2010 - Elsevier
     
    2. Structures of the first representatives of Pfam family PF06938 (DUF1285) reveal a new fold with repeated structural motifs and possible involvement in signal
    GW Han, C Bakolitsa, MD Miller, A Kumar - Section F: Structural , 2010 - scripts.iucr.org
     
    3. NMR structure of protein PA2021 from Pseudomonas aeruginosa
    YC Lin, G Liu, Y Shen, C Bertonati - Proteins: Structure, , 2006 - Wiley Online Library
     

    Protein Summary

    PA2021 is the first structural representative of a small family specific to Pseudomonas aeruginosa. pre-SCOP classifies PA2021 as having a PH domain-like fold. A search with DaliLite shows the closest structural similarity to be with two members of the DUF1285 family (PDB id: 2ra9, 2re3) with backbone rmsd of 3.2 Å and 3.5 Å over 55 and 62 residues and sequence identity of 11% and 16% respectively (Z scores 3.7 and 3.4). Other high-scoring hits include the Ras-related protein Ral-A (PDB id: 1zc3, rmsd 2.5 Å over 59 residues, 10% sequence id, Z-score 3.4), TBC1 domain 2 (PDB id: 2dhk), a member of the DUF1696 family (PDB id: 3dcx), neurofibromin domains (PDB ids: 2e2x and 2d4q with rmsd 2.5 Å over 56 residues, 13% sequence id, Z-score 3.2), Rho GEF (guanine exchange nucleotide factor) 12 (PDB id: 1x86), pleckstrin (PDB id: 1zm0) and other PH domains. A superposition of PA2021 and Ral-A is shown in Fig. 1. With the exception of the first β-strand in Ral-A, all other secondary structure elements, topology and tertiary arrangements are replicated in PA2021.  

    1ywy1zc3_stereo.png

    Figure 1. Stereo-view in ribbon diagram showing the superposition of PA2021 (Pdb id: 1ywy) and Ral-A (Pdb id: 1zc3).

     

    Pleckstrin homology (PH) domains (Pfam PF00169) are found in a wide range of eukaryotic proteins implicated in cell-signaling (Mayer 1993, Ingley 1994) and the cytoskeleton (Lemmon 2002). PH domains bind phosphatidylinositol lipids (Lemmon 2003), heterotrimeric G proteins (LeVine 1999) and protein kinase C [refs]. Through these interactions, PH domains help recruit proteins to different membranes, thus targeting them to appropriate cellular compartments or enabling them to interact with other components of signal transduction pathways. All known cases have a common structure consisting of two perpendicular anti-parallel β sheets, followed by a C-terminal amphipathic helix. The C-terminal part of the PH domain has been implicated in G-protein binding (Touhara 1994) while the β loops have been implicated in phosphoinositide binding (DiNitto 2006). The loops connecting the β-strands differ greatly in length, making the PH domain relatively difficult to detect while providing the source of the domain's specificity (DiNitto 2006). The only conserved residue among PH domains is a single tryptophan located within the α-helix that serves to nucleate the core of the domain ().

     

    The gene neighborhood of PA2021 suggests a functional association with UDP-glucose 6-dehydrogenase (EC 1.1.1.22) and UTP-glucose-1-phosphate uridylyltransferase (EC 2.7.7.9).

    Ligand Summary

    Reviews

    References

     

    No references found.

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    106.72 kB18:40, 10 Dec 2008tinabActions
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