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

    Title Crystal structure of acetoin utilization protein (ZP_00540088.1) from Exiguobacterium sibiricum 255-15 at 2.33 A resolution. To be published
    Site JCSG
    PDB Id 2q04 Target Id 370251
    Molecular Characteristics
    Source Exiguobacterium sibiricum 255-15
    Alias Ids TPS1557,YP_001814707.1, 91191 Molecular Weight 24067.36 Da.
    Residues 210 Isoelectric Point 5.37
    Sequence mfekqfnhrtletslgpveiegpvtsqilatykldpgltafrqpaeqhealveiaaleegriiiarqgn diigyvtflypdpyetwsegnnpyilelgaievaarfrgqqigkkllevsmldpamehyliltteyywh wdlkgsglsvwdyrkimekmmnhgglvffptddpeiashpanclmarigkhvapevvahfdalrlrrrf myd
      BLAST   FFAS

    Structure Determination
    Method XRAY Chains 6
    Resolution (Å) 2.33 Rfree 0.260
    Matthews' coefficent 3.18 Rfactor 0.229
    Waters 240 Solvent Content 61.36

    Ligand Information


    Google Scholar output for 2q04
    1. 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
    2. Biochemical and mutational analyses of AcuA, the acetyltransferase enzyme that controls the activity of the acetyl coenzyme a synthetase (AcsA) in Bacillus subtilis
    JG Gardner, JC Escalante-Semerena - Journal of bacteriology, 2008 - Am Soc Microbiol
    3. Biochemical and mutational analyses of AcuA, the acetyltransferase enzyme that controls the activity of the acetyl-CoA synthetase (AcsA) in Bacillus subtilis
    JG Gardner, JC Escalante-Semerena - 2008 - Am Soc Microbiol
    4. Genetics and biochemistry of acetyl-coenzyme A synthetase post-translational control in Bacillus subtilis
    JG Gardner - 2008 - books.google.com

    Protein Summary

    The Exig_2238 gene from Exiguobacterium sp. 255-15 encodes an acetoin utilization protein (PF00583, cl00443) found in all domains of life. The structure adopts an alpha-beta-alpha sandwich with aminopeptidase fold and is similar to several other PSI structures solved from the same family (PDB ids 3BLN, 3D3S, 1Y9K, 3EO4, 2Q7B, 2QEC).

    Acetoin (3-hydroxy-2-butanone) is secreted by bacteria in the media during growth but can be reutilized under conditions of glucose starvation, or generally when other nutrients are scarce. It is used for the production of acetyl-CoA, similar to pyruvate. 1q04 is similar to AcuA from several organisms, part of the acuABC (not to be confused with the AcoABCL complex) operon involved in acetoin reutilization[Ref]. Although AcuA is often labeled as acetoin dehydrogenase, its role appears that of regulating the activity of the acetyl-CoA synthetase AcsA by acetylation, hence its sequence and structural similarity with GNAT-family acetyltranferases. Unlike most of these however, the flap domain that covers the putative active site consists of a loop between the beta5 strand and the alpha5 helix. This structure was used as the basis for a mutational analysis of B. subtilis AcuA[Ref]. For more information on the role of acetoin in bacteria see [Ref].

    To do: look at oligomerization interface, binding sites, residue conservation etc.

    Ligand Summary





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