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Adenovirus proteinase: crystallization and preliminary X-ray diffraction studies to atomic resolution
Mary Lynn Baniecki1, William J McGrath, Zbigniew Dauter
1Department of Pharmacological Sciences, State University of New York at Stony Brook, 11794, USA.
Acta Crystallographica. Section D, Biological Crystallography
|August 29, 2002
Summary
Adenovirus proteinase (AVP) structure was determined without cofactors. This provides a basis for understanding how cofactors activate this antiviral therapy target.
Area of Science:
- Biochemistry
- Structural Biology
- Virology
Background:
- Adenovirus proteinase (AVP) is crucial for infectious adenovirus synthesis.
- AVP requires viral cofactors, pVIc peptide and viral DNA, for activation.
- The apo-structure of AVP, without cofactors, has not been previously determined.
Purpose of the Study:
- To determine the crystal structure of Adenovirus proteinase (AVP) in its unactivated state.
- To provide a structural basis for understanding AVP activation by its cofactors.
Main Methods:
- Single crystals of AVP were obtained using microseeding and hanging-drop vapour-diffusion.
- Sodium acetate and sodium citrate were used as precipitants.
- X-ray diffraction data were collected at the National Synchrotron Light Source.
Main Results:
- The native crystal diffracted to a high resolution of 0.98 Å.
- An isomorphous heavy-atom derivative diffracted to 1.9 Å.
- The apo-structure of AVP was successfully determined.
Conclusions:
- The determined apo-structure of AVP serves as a critical reference point.
- Comparison with the AVP-pVIc complex structure will elucidate the mechanism of cofactor-mediated activation.
- This structural insight is vital for developing targeted antiviral therapies against adenovirus.