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3eua

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

    Title Crystal structure of yurp protein (np_391141.1) from bacillus subtilis at 1.90 A resolution. To be published
    Site JCSG
    PDB Id 3eua Target Id 390575
    Molecular Characteristics
    Source Bacillus subtilis subsp. subtilis str. 168
    Alias Ids TPS14584,NP_391141.1, 3.40.50.10490, 104594 Molecular Weight 36873.88 Da.
    Residues 328 Isoelectric Point 5.54
    Sequence msqatakvnrevqaflqdlkgktidhvffvacggssaimypskyvfdresksinsdlysanefiqrnpv qlgekslvilcshsgntpetvkaaafargkgaltiamtfkpesplaqeaqyvaqydwgdealaintnyg vlyqivfgtlqvlenntkfeqaiegldqlqavyekalkqeadnakqfakahekesiiytmasganygva ysysicilmemqwihshaihageyfhgpfeiidesvpfiillgldetrpleeraltfskkygkkltvld aasydftaiddsvkgylaplvlnrvlrsyadelaeernhplshrrymwkvey
      BLAST   FFAS

    Structure Determination
    Method XRAY Chains 8
    Resolution (Å) 1.90 Rfree 0.212
    Matthews' coefficent 2.03 Rfactor 0.168
    Waters 1708 Solvent Content 39.48

    Ligand Information
    Ligands
    Metals

    Jmol

     
    Google Scholar output for 3eua

    Protein Summary

    Gene BSU32610 encodes NP_391141.1, a protein with 328 residues from Bacillus subtilis, a Gram-positive and catalase-positive bacterium commonly found in soil.  The results from NCBI sequence alignments suggests that this protein may be a sugar isomerase, which belongs to the SIS domain family (PF01380). In the conserved isomerase domain, Ser 81, Ser 83, Thr 86, His82, Ser35 may be involved in the H-Bonding network for sugar substrates binding. There are eight  3eua molecules in each asymmetric unit.  The interface interaction suggests that the biomolecule of 3eua may be a dimer.

      

    390575_1.png

      

    Figure 1. The 3eua molecule consists of two domains. The conserved isomerase domain

    locates in the N-terminal domain and near to the interface of two domains. 

      

    390575_2.png

      

     Figure 2. The biomolecule of 3eua is a dimer based on the interface interaction.

      

    390575_3.png

      

    Figure 3. 3eua (green) is structurally similar to 1M0R, 2AML, 2PUV

    and 2VF5 with a conserved isomerase catalytic site. 

      

    390575_4.png

      

    Figure 4. In the conserved sugar isomerase domain of 3eua, residues Ser 81, Ser 83,

    Thr 86, His82, Ser35 maybe involved in a H-bond network for sugar substrates binding.  

      

      

      

    References

      

    1.    Raczynska, J.,  Olchowy, J.,  Konariev, P.V.,  Svergun, D.I.,  Milewski, S.,  Rypniewski, W.   (2007) The Crystal and Solution Studies of Glucosamine-6-phosphate Synthase from Candida albicans  J.Mol.Biol.   372: 672-688   (PDB: 2PUV).

    2.    Teplyakov, A.,  Obmolova, G.,  Badet-Denisot, M.A.,  Badet, B.,  Polikarpov, I.  (1998) Involvement of the C terminus in intramolecular nitrogen channeling in glucosamine 6-phosphate synthase: evidence from a 1.6 A crystal structure of the isomerase domain.  Structure   6: 1047-1055   (PDB ID: 1MOR)

    3.    Teplyakov, A.,  Obmolova, G.,  Badet-Denisot, M.A.,  Badet, B.   (1999) The mechanism of sugar phosphate isomerization by glucosamine 6-phosphate synthase.  Protein Sci.   8: 596-602   (PDB 1MOS)

    Ligand Summary

    Citrate anions

    Glycerin 

    Reviews

    References

     

    No references found.

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