The Open Protein Structure Annotation Network
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    Table of contents
    1. 1. Protein Summary
    2. 2. Ligand Summary
    3. 3. References

    Title Crystal structure of Anthranilate phosphoribosyltransferase 2 (17130499) from Nostoc sp. at 1.85 A resolution. To be published
    Site JCSG
    PDB Id 1vqu Target Id 354074
    Molecular Characteristics
    Source Nostoc sp. pcc 7120
    Alias Ids TPS1320,17130499 Molecular Weight 37595.68 Da.
    Residues 362 Isoelectric Point 4.99
    Sequence mtssptstqesstswylllqqlidgeslsrsqaaelmqgwlseavppelsgailtalnfkgvsadeltg maevlqsqskmgtgenysqlpitnspfsiidtcgtggdgsstfnistavafvaaaygvpvakhgnrsas sltgsadvlealgvnlgaspekvqaalqevgitflfapgwhpalkavatlrrtlrirtvfnllgplvnp lrptgqvvglftpkllttvaqaldnlgkqkaivlhgrerldeaglgdltdlavlsdgelqlttinpqev gvtpapigalrggdvqenaeilkavlqgkgtqaqqdavalnaalalqvagavplldhaqgvsvakeilq tgtawaklaqlvyflgn
      BLAST   FFAS

    Structure Determination
    Method XRAY Chains 2
    Resolution (Å) 1.85 Rfree 0.2206
    Matthews' coefficent 2.23 Rfactor 0.17921
    Waters 232 Solvent Content 44.47

    Ligand Information


    Google Scholar output for 1vqu
    1. An iterative knowledge_based scoring function for proteinprotein recognition
    SY Huang, X Zou - Proteins: Structure, Function, and , 2008 - Wiley Online Library
    2. Evaluating the usefulness of protein structure models for molecular replacement
    A Giorgetti, D Raimondo, AE Miele - Bioinformatics, 2005 - Oxford Univ Press
    3. Domain definition and target classification for CASP6
    M Tress, CH Tai, G Wang, I Ezkurdia - PROTEINS: , 2005 - Wiley Online Library
    4. Fast and accurate algorithms for protein side-chain packing
    J Xu, B Berger - Journal of the ACM (JACM), 2006 - dl.acm.org
    5. Developing a move-set for protein model refinement
    MN Offman, PW Fitzjohn, PA Bates - Bioinformatics, 2006 - Oxford Univ Press
    6. Protein structure prediction in CASP6 using CHIMERA and FAMS
    M Takeda_Shitaka, G Terashi, D Takaya - PROTEINS: , 2005 - Wiley Online Library
    7. A rationally designed monomeric variant of anthranilate phosphoribosyltransferase from Sulfolobus solfataricus is as active as the dimeric wild-type enzyme but less
    T Schwab, D Skegro, O Mayans, R Sterner - Journal of molecular biology, 2008 - Elsevier
    8. Post to
    A Paiardini, R Sali, F Bossa - BMC structural , 2008 - biomedcentral.com
    9. Structural and mutational analysis of substrate complexation by anthranilate phosphoribosyltransferase from Sulfolobus solfataricus
    M Marino, M Deuss, DI Svergun, PV Konarev - Journal of Biological , 2006 - ASBMB
    10. Prediction of protein domain boundaries from statistics of appearance of amino acid residues
    OV Galzitskaya, NV Dovidchenko, MY Lobanov - Molecular Biology, 2006 - Springer
    11. Protein structure prediction based on the sliced lattice model
    CC Wang, CB Yang, HY Ann - 2008 Conference on , 2005 - etd.lib.nsysu.edu.tw
    12. Activation of anthranilate phosphoribosyltransferase from Sulfolobus solfataricus by removal of magnesium inhibition and acceleration of product release
    S Schlee, M Deuss, M Bruning, A Ivens, T Schwab - Biochemistry, 2009 - ACS Publications
    13. Prediction of Protein Backbone Based on the Sliced Lattice Model
    CC Wang, CB Yang, HY Ann, HY Chang - 2008 - csie.npu.edu.tw
    14. Stabilization of a Metabolic Enzyme by Library Selection in Thermus thermophilus
    T Schwab, R Sterner - ChemBioChem, 2011 - Wiley Online Library

    Protein Summary

    The gene 17130499 from Nostoc sp. encodes an enzyme anthranilate phosphoribosyltransferase EC: COG0547, a member of glycosyl transferase family PF02885.  Alternative names: phosphoribosyl-anthranilate diphosphorylase, phosphoribosyl-anthranilate pyrophosphorylase.  The enzyme belongs to the class of all alpha proteins and reveals methionine synthase domain-like fold type SCOP47643.  The enzyme catalyzes the following reaction: N-(5-phospho-D-ribosyl)-anthranilate + diphosphate <=> anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate.  The biological unit of the enzyme is a homodimer.  In some organisms, this enzyme is part of a multifunctional protein together with one or more components of the system for biosynthesis of phenylalanine, tyrosine and tryptophan.  The structure of the enzyme homologue from Pectobacterium carotovorum has been previously solved 1KHD. There is also a holo structure from Mycobacterium tuberculosis, 1zvw, solved and published [Ref] by TBSGC with the alpha-phosphoribosylpyrophosphoric acid ligand bound. A structure comparison of 1vqu (chain B) and 1zvw (chain A) with TopMatch results in 310 equivalent residus at an rmsd of 1.63A and 39% sequence identity.

    Ligand Summary





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