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Published on: July 5, 2018
Recombinant bovine uteroglobin at 1.6 A resolution: a preliminary X-ray crystallographic analysis
Victoria von der Decken1, Heinrich Delbrück, Andreas Herrler
1Institute of Anatomy and Reproductive Biology, Medical School RWTH Aachen, Wendlingweg 2, 52074 Aachen, Germany.
Insights
Researchers crystallized recombinant bovine uteroglobin (recbUG) in two forms, rhomboid and cuneate. These crystal structures provide insights into uteroglobin
Area of Science:
- Structural biology
- Protein crystallography
- Biochemistry
Background:
- Uteroglobin (UG) is a progesterone-induced protein secreted by mammalian reproductive and respiratory epithelia.
- Its precise biological functions are still under investigation, highlighting the need for structural data.
Purpose of the Study:
- To obtain high-resolution crystal structures of recombinant bovine uteroglobin (recbUG).
- To characterize the crystallographic properties of recbUG in different geometric forms.
Main Methods:
- Overexpression and purification of recombinant bovine uteroglobin (recbUG) in E. coli.
- Crystallization of recbUG using the hanging-drop vapor-diffusion method.
- X-ray diffraction analysis of rhomboid and cuneate crystal forms using synchrotron radiation and a rotating-anode generator.
Main Results:
- Two distinct crystal forms of recbUG were obtained: rhomboid and cuneate.
- Rhomboid crystals diffracted to 1.6 A resolution in space group P2(1)2(1)2, containing four monomers per asymmetric unit.
- Cuneate crystals diffracted to 2.35 A resolution in space group C222(1), containing two molecules per asymmetric unit.
Conclusions:
- Successful crystallization and structural determination of recbUG in two distinct forms.
- The obtained crystallographic data provide a foundation for further structural and functional studies of uteroglobin.
Abstract:
Uteroglobin (UG) is a conserved protein which is induced by progesterone and secreted by the epithelia of various mammalian reproductive and respiratory organs. Recombinant bovine uteroglobin (recbUG), consisting of 80 amino acids with a C-terminal His6 tag, was overexpressed in Escherichia coli and purified. The protein was crystallized in two geometric forms, rhomboid and cuneate (wedge-shaped), by the hanging-drop vapour-diffusion method at 295 K. The rhomboid crystals diffracted to a maximum resolution of 1.6 A using synchrotron radiation. These crystals belong to space group P2(1)2(1)2, with unit-cell parameters a = 81.42, b = 82.82, c = 45.26 A, and contain four monomers per asymmetric unit. The cuneate crystals diffracted to 2.35 A resolution using a rotating-anode generator. These crystals belong to space group C222(1), with unit-cell parameters a = 43.39, b = 93.94, c = 77.30 A, and contain two molecules per asymmetric unit.
