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1vli

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

    Title Crystal structure of Spore coat polysaccharide biosynthesis protein spsE (BSU37870) from Bacillus subtilis at 2.38 A resolution. To be published
    Site JCSG
    PDB Id 1vli Target Id 355716
    Molecular Characteristics
    Source Bacillus subtilis subsp. subtilis str. 168
    Alias Ids TPS1349,2636322, PF06981 Molecular Weight 40887.44 Da.
    Residues 373 Isoelectric Point 5.37
    Sequence maafqianktvgkdapvfiiaeaginhdgkldqafalidaaaeagadavkfqmfqadrmyqkdpglykt aagkdvsifslvqsmempaewilplldycrekqviflstvcdegsadllqstspsafkiasyeinhlpl lkyvarlnrpmifstagaeisdvheawrtiraegnnqiaimhcvakypappeysnlsvipmlaaafpea vigfsdhsehpteapcaavrlgakliekhftidknlpgadhsfalnpdelkemvdgirkteaelkqgit kpvsekllgssyktttaiegeirnfayrgifttapiqkgeafsedniavlrpgqkpqglhprffellts gvravrdipadtgivwddillkdspfhe
      BLAST   FFAS

    Structure Determination
    Method XRAY Chains 1
    Resolution (Å) 2.38 Rfree 0.23799
    Matthews' coefficent 3.74 Rfactor 0.19035
    Waters 83 Solvent Content 66.82

    Ligand Information
    Ligands
    Metals

    Jmol

     
    Google Scholar output for 1vli
    1. The Buccaneer software for automated model building. 1. Tracing protein chains
    K Cowtan - Acta Crystallographica Section D: Biological , 2006 - scripts.iucr.org
     
    2. Exploiting heterogeneous sequence properties improves prediction of protein disorder
    Z Obradovic, K Peng, S Vucetic - Proteins: Structure, , 2005 - Wiley Online Library
     
    3. 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
     
    4. Domain definition and target classification for CASP6
    M Tress, CH Tai, G Wang, I Ezkurdia - PROTEINS: , 2005 - Wiley Online Library
     
    5. Fast and accurate algorithms for protein side-chain packing
    J Xu, B Berger - Journal of the ACM (JACM), 2006 - dl.acm.org
     
    6. Prediction of protein domain boundaries from statistics of appearance of amino acid residues
    OV Galzitskaya, NV Dovidchenko, MY Lobanov - Molecular Biology, 2006 - Springer
     
    7. Protein Structure Prediction Using a Profile-Profile Comparison Method: FORTE
    _____ - ____, 2006 - J-STAGE
     
    8. Structural Survey of Zinc-Containing Proteins and Development of the Zinc AMBER Force Field (ZAFF)
    MB Peters, Y Yang, B Wang - Journal of chemical , 2010 - ACS Publications
     

    Protein Summary

    The gene 2636322 from Bacillus subtilis encodes a putative N-acetylneuraminic acid (Neu5Ac) synthase EC:2.5.1.57 COG2089, a member of NeuB family PF03102.  Alternative names: N-acetylneuraminate 9-phosphate lyase, sialic acid 9-phosphate synthetase.  The enzyme belongs to the class of alpha and beta (a+b) proteins and reveals TIM beta/alpha-barrel SCOP51350.  The enzyme catalyzes the following reaction: phosphoenolpyruvate + N-acyl-D-mannosamine 6-phosphate + H(2)O <=> N-acylneuraminate 9-phosphate + phosphate.  Sialic acid or N-acetylneuraminic acid (NeuAc) plays a wide variety of important biological roles. In mammals, it is found as the terminal carbohydrate residue of many cell surface glycoconju- gates. Thus, its structure defines the periphery of mammalian cells, and it is a key determinant in mediating cellular recognition processes. These include the binding between selectins and leukocytes in the inflammation response (5) and the binding of the influenza virus and mammalian cells during infection. While sialic acid is not commonly found in prokaryotes, certain pathogenic bacteria biosynthesize it as a virulence factor [Ref].  Thus, it is an attractive drug target.  For instance, the structure of the enzyme homologue from Neisseria meningitidis in complex with its first potent inhibitor has been recently determined 2WQP.

    Ligand Summary



    References

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