Small-angle X-ray Scattering Studies of the Oligomeric State and Quaternary Structure of the Trifunctional Proline Utilization A (PutA) Flavoprotein from \u3ci\u3eEscherichia coli\u3c/i\u3e

  • Singh, Ranjan K.
  • Larson, John D.
  • Zhu, Weidong
  • Rambo, Robert P.
  • Hura, Greg L.
  • Becker, Donald F.
  • Tanner, John J.
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Publication date
June 2016
Publisher
DigitalCommons@University of Nebraska - Lincoln
Language
English

Abstract

Background: Trifunctional proline utilization A (PutA) proteins are multifunctional flavoproteins that catalyze two reactions and repress transcription of the put regulon. Results: PutA from Escherichia coli is a V-shaped dimer, with the DNA-binding domain mediating dimerization. Conclusion: Oligomeric state and quaternary structures are not conserved by PutAs. Significance: The first three-dimensional structural information for any trifunctional PutA is reported

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