Details

Autor(en) / Beteiligte

• Welner, Ditte Hededam
• Tsai, Alex Yi-Lin
• DeGiovanni, Andy M.
• Scheller, Henrik Vibe
• Adams, Paul D.

Titel

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

Ist Teil von

• Acta crystallographica. Section F, Structural biology communications, 2017-03, Vol.73 (4)

Ort / Verlag

United States: International Union of Crystallography

Erscheinungsjahr

2017

Quelle

Wiley-Blackwell Journals

Beschreibungen/Notizen

• 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 fromOryza 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.