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

    Title Crystal structure of Gamma-glutamyl phosphate reductase (yor323c) from Saccharomyces cerevisiae at 2.40 A resolution. To be published
    Site JCSG
    PDB Id 1vlu Target Id 354122
    Molecular Characteristics
    Source Saccharomyces cerevisiae
    Alias Ids TPS1321,YOR323C Molecular Weight 49866.35 Da.
    Residues 457 Isoelectric Point 5.37
    Sequence msssqqiaknarkagnilktisnegrsdilykihdalkanahaieeankidlavaketgladsllkrld lfkgdkfevmlqgikdvaeledpvgkvkmarelddgltlyqvtapvgvllvifesrpevianitalsik sgnaailkggkesvntfremakivndtiaqfqsetgvpvgsvqlietrqdvsdlldqdeyidlvvprgs nalvrkikdttkipvlghadgicsiyldedadlikakrisldaktnypagcnametllinpkfskwwev lenltleggvtihatkdlktayfdklnelgklteaiqcktvdadeeqdfdkeflsldlaakfvtstesa iqhinthssrhtdaivtenkanaekfmkgvdssgvywnastrfadgfrygfgaevgistskihargpvg ldglvsyqyqirgdgqvasdylgaggnkafvhkdldiktvtlz
      BLAST   FFAS

    Structure Determination
    Method XRAY Chains 2
    Resolution (Å) 2.29 Rfree 0.24782
    Matthews' coefficent 3.58 Rfactor 0.21043
    Waters 124 Solvent Content 65.60

    Ligand Information


    Google Scholar output for 1vlu
    1. The Buccaneer software for automated model building. 1. Tracing protein chains
    K Cowtan - Acta Crystallographica Section D: Biological , 2006 - scripts.iucr.org
    2. Structural biology of proline catabolism
    JJ Tanner - Amino acids, 2008 - Springer
    3. Pyrroline_5_carboxylate synthase and proline biosynthesis: From osmotolerance to rare metabolic disease
    I Prez_Arellano, F Carmona_lvarez - Protein , 2010 - Wiley Online Library
    4. Comprehensive analysis of the helix_X_helix motif in soluble proteins
    J Deville, J Rey, M Chabbert - Proteins: Structure, Function, and , 2008 - Wiley Online Library
    5. Etude structurale des cassures d'hlices et son application la modlisation des rcepteurs coupls aux protines G (RCPG)
    J Devill - 2007 - hal.archives-ouvertes.fr

    Protein Summary

    The gene ID YOR323C from Saccharomyces cerevisiae (budding yeast) encodes the enzyme gamma-glutamyl phosphate reductase (GPR) E.C. PF00171 COG0014.  The enzyme belongs to aldehyde dehydrogenase families 18 and 19, a superfamily of oxidoreductases.  The enzyme is involved in amino acid metabolism and catalyzes the second step in proline biosynthesis from glutamate.  The closest orthologue is glutamate-5-semialdehyde dehydrogenase.  The catalyzed reaction is the NADP-dependent reduction of L-glutamate 5-phosphate into L-glutamate 5-semialdehyde and phosphate.  The structure of the enzyme homologue from Thermotoga maritima (TM0293) has been previously solved 1O20. This family of enzymes is generally dimeric or tetrameric, each subunit consisting of a dinucleotide binding domain resembling a Rossmann fold and  a catalytic alpha/beta domain, plus a small dimerization/tetramerization module that accounts for a large fraction of the intersubunit binding surface. 1VLU appears unique in the relative orientation of the two subunits, which results in a remarkably more open dimer that adopt an almost flat rather, than globular, shape. The dimer possibly further arranges into a novel tetrameric assembly. Yeast GPR is monofunctional [Ref], while in plants and mammals its bifunctional and consists of  N-terminal glutamate 5-kinase domain and a C-terminal GPR domain [Ref].

    Ligand Summary





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