Structure of a xenon derivative of Escherichia coli copper amine oxidase: confirmation of the proposed oxygen-entry pathway
2008
Structure of a xenon derivative of E. coli copper amine oxidase
publication
Evidence: high
Author Information
Author(s): Pirrat Pascale, Smith Mark A., Pearson Arwen R., McPherson Michael J., Phillips Simon E. V.
Primary Institution: Astbury Centre for Structural Molecular Biology, University of Leeds
Hypothesis
Does the presence of the N-terminal domain in E. coli copper amine oxidase affect the molecular oxygen entry pathway?
Conclusion
The study confirms that the N-terminal domain does not affect oxygen entry in E. coli copper amine oxidase.
Supporting Evidence
- The study used xenon as a probe to investigate oxygen entry pathways.
- X-ray crystallography revealed the structure of the enzyme at high resolution.
- The findings are consistent with previous studies on other copper amine oxidases.
Takeaway
Scientists looked at a special version of an enzyme to see how oxygen gets in. They found that a part of the enzyme doesn't change how oxygen enters.
Methodology
The structure was determined using X-ray crystallography at 2.5 Å resolution after xenon derivatization.
Digital Object Identifier (DOI)
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