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X-ray diffraction analysis and in vitro characterization of the UAM2 protein from Oryza sativa

  • Author(s): Welner, DH
  • Tsai, AYL
  • Degiovanni, AM
  • Scheller, HV
  • Adams, PD
  • et al.

Published Web Location

http://journals.iucr.org/f/issues/2017/04/00/hv5349/hv5349.pdf
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Abstract

© Welner et al. 2017. The role of seemingly non-enzymatic proteins in complexes interconverting UDP-arabinopyranose and UDP-arabinofuranose (UDP-arabinosemutases; UAMs) in the plant cytosol remains unknown. To shed light on their function, crystallographic and functional studies of the seemingly non-enzymatic UAM2 protein from Oryza sativa (OsUAM2) were undertaken. Here, X-ray diffraction data are reported, as well as analysis of the oligomeric state in the crystal and in solution. OsUAM2 crystallizes readily but forms highly radiation-sensitive crystals with limited diffraction power, requiring careful low-dose vector data acquisition. Using size-exclusion chromatography, it is shown that the protein is monomeric in solution. Finally, limited proteolysis was employed to demonstrate DTT-enhanced proteolytic digestion, indicating the existence of at least one intramolecular disulfide bridge or, alternatively, a requirement for a structural metal ion.

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