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    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,, 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


    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.




    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. 




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




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

    and 2VF5 with a conserved isomerase catalytic site. 




    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.  






    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





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