Small-angle X-ray Scattering Studies of the Oligomeric State and Quaternary Structure of the Trifunctional Proline Utilization A (PutA) Flavoprotein from Escherichia coli

Authors

• Ranjan K. Singh, University of Missouri-Columbia
• John D. Larson, University of Missouri-Columbia
• Weidong Zhu, University of Nebraska - Lincoln
• Robert P. Rambo, Lawrence Berkeley National Laboratory, Berkeley
• Greg L. Hura, Lawrence Berkeley National Laboratory, Berkeley
• Donald F. Becker, University of Nebraska-LincolnFollow
• John J. Tanner, University of Missouri-Columbia, Columbia, MOFollow

Document Type

Article

Citation

J. Biol. Chem. 2011, 286:43144-43153.

doi: 10.1074/jbc.M111.292474 originally published online October 19, 2011

Comments

Printed in the U.S.A.

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.