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The Open Protein Structure Annotation Network
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3get

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

    Title Crystal structure of putative histidinol-phosphate aminotransferase (NP_281508.1) from Campylobacter jejuni at 2.01 A resolution. To be published
    Site JCSG
    PDB Id 3get Target Id 390730
    Molecular Characteristics
    Source Campylobacter jejuni subsp. jejuni nctc 11168
    Alias Ids TPS14610,NP_281508.1, 3.40.640.10, 85760 Molecular Weight 41366.10 Da.
    Residues 364 Isoelectric Point 5.83
    Sequence mkfneflnnlsnyepgkdieviakeygvkeviklasnenpfgtppkaieclrqnankahlypddsmiel kstlaqkykvqneniiigagsdqviefaihsklnsknaflqagvtfamyeiyakqcgakcyktqsithn ldefkklyethkdeikliflclpnnplgecldaseatefikgvnedclvvidaaynefasfkdskkhle pcelikefdnvlylgtfsklyglgglrigygiananiisafyklrapfnvsnlalkaavaamdddefte ktlennfsqmelykefakkhnikiidsytnfityffdeknstdlsekllkkgiiirnlksyglnairit igtsyenekfftefdkilr
      BLAST   FFAS

    Structure Determination
    Method XRAY Chains 2
    Resolution (Å) 2.01 Rfree 0.235
    Matthews' coefficent 2.12 Rfactor 0.174
    Waters 565 Solvent Content 42.07

    Ligand Information
    Ligands
    Metals

    Jmol

     
    Google Scholar output for 3get

    Protein Summary

    Pfam: this protein is reassigned to Aminotran_1_2, CL0061, which has other structures.

     

    NP_281508.1 is a protein with 364 residues from CAMPYLOBACTER JEJUNI, which is a Gram-negative microaerophilic bacteria commonly found in animal feces.  The results from NCBI sequence alignments suggests that this protein be a sequence homolog to histidinol-phosphate aminotransferase, which belongs to Pfam 00155.  Structural conserved residues, including Tyr 61, Asp 91, Tyr 115, Tyr 121, Asp 190, Tyr 193, Ser 225, Lys 226, Arg 234, and Tyr 337, sketches a fairly hydrophobic and tyrosine-riched active site for substrate adaptation.  This conserved active site locates on the interface between two subunits. In each subunit, one PLP molecule from protein  expression is modeled and linked to the Lys226 in Schiff Base format in this conserved active site. The interface interaction suggests that the biomolecule of NP_281508.1 be a dimer.

     

     

    390730_1.png

     

    Figure 1. Protein NP_281508.1 molecule carries a conserved tyrosine-riched active site for substrate adoption. 

     

    390730_2.png

     

    Figure 2.  The biomolecule of NP_281508.1 is a dimer based on interface interaction.

     

    390730_3.png

     

    Figure 3. Protein NP_281508.1 (Magenta) is structural homolog to 1FG3(cyan), 1GEW(yellow), 1LC5(orange) and 1UU0( blue) with highly structural conserved residues.  

     

    This putative histidinol-phosphate aminotransferase, according to predictions from STRING server, is functionally associated with enzymes from phenylalanine metabolism, and biosynthesis of phenylalanine, tyrosine and tryptophan.

     

    Literature

    1.    Ko TP, Wu SP, Yang WZ, Tsai H, Yuan HS; , Acta Crystallogr D Biol Crystallogr 1999;55:1474-1477.: Crystallization and preliminary crystallographic analysis of the Escherichia coli tyrosine aminotransferase

    2.    Nakai T, Okada K, Akutsu S, Miyahara I, Kawaguchi S, Kato R, Kuramitsu S, Hirotsu K; , Biochemistry 1999;38:2413-2424.: Structure of Thermus thermophilus HB8 aspartate aminotransferase and its complex with maleate

    3.    Fernandez, F.J.,  Vega, M.C.,  Lehmann, F.,  Sandmeier, E.,  Gehring, H.,  Christen, P.,  Wilmanns, M.   (2004) Structural studies of the catalytic reaction pathway of a hyperthermophilic histidinol-phosphate aminotransferase.  J.Biol.Chem.   279: 21478-21488   (PDB ID: 1UU0, 1H1C, 1UU1, 1UU2).

     

     

     

     

    Ligand Summary

     2-propanol and glycerol molecules.

    Reviews

    References

     

    No references found.

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