Article
The N-terminal coiled coil of the Rhodococcus erythropolis ARC AAA ATPase is neither necessary for oligomerization nor nucleotide hydrolysis.
Journal of structural biology - 1 Jan 2000
Zhang Xujia, Stoffels Katinka, Wurzbacher Stephanie, Schoofs Geert, Pfeifer Günter, Banerjee Tisha, Parret Annabel H A, Baumeister Wolfgang, De Mot René, Zwickl Peter
Abstract excerpt
Deletion mutants of the Rhodococcus erythropolis ARC AAA ATPase were generated and characterized by biochemical analysis and electron microscopy. Based on sequence comparisons the ARC protein was divided into three consecutive regions, the N-terminal coiled coil, the central ARC-specific inter domain and the C-terminal AAA domain. When the ARC AAA domain was expressed separately it formed aggregates of undefined...
Topics
- Adenosine Triphosphatases
- Amino Acid Sequence
- Crystallization
- Dimerization
- Mutation
- Nucleotides
- Peptide Fragments
- Protein Structure, Quaternary
- Protein Structure, Tertiary
- Rhodococcus