Journal article
The structure of Aquifex aeolicus FtsH in the ADP-bound state reveals a C2-symmetric hexamer.
- Vostrukhina M Department of Chemistry and Biochemistry, University of Bern, Freiestrasse 3, Bern, CH-3012, Switzerland.
- Popov A European Synchrotron Radiation Facility, 6 Rue Jules Horowitz, Grenoble, F-38043, France.
- Brunstein E Institute of Biochemistry, University of Cologne, Otto-Fischer-Strasse 12-14, Cologne, D-50674, Germany.
- Lanz MA Department of Chemistry and Biochemistry, University of Bern, Freiestrasse 3, Bern, CH-3012, Switzerland.
- Baumgartner R Department of Chemistry and Biochemistry, University of Bern, Freiestrasse 3, Bern, CH-3012, Switzerland.
- Bieniossek C Department of Chemistry and Biochemistry, University of Bern, Freiestrasse 3, Bern, CH-3012, Switzerland.
- Schacherl M Institute of Biochemistry, University of Cologne, Otto-Fischer-Strasse 12-14, Cologne, D-50674, Germany.
- Baumann U Institute of Biochemistry, University of Cologne, Otto-Fischer-Strasse 12-14, Cologne, D-50674, Germany.
- 2015-06-10
Published in:
- Acta crystallographica. Section D, Biological crystallography. - 2015
AAA protease
crystal disorder
metalloprotease
Adenosine Diphosphate
Bacteria
Bacterial Proteins
Crystallization
Crystallography, X-Ray
Models, Molecular
Protein Conformation
English
The crystal structure of a truncated, soluble quadruple mutant of FtsH from Aquifex aeolicus comprising the AAA and protease domains has been determined at 2.96 Å resolution in space group I222. The protein crystallizes as a hexamer, with the protease domain forming layers in the ab plane. Contacts between these layers are mediated by the AAA domains. These are highly disordered in one crystal form, but are clearly visible in a related form with a shorter c axis. Here, adenosine diphosphate (ADP) is bound to each subunit and the AAA ring exhibits twofold symmetry. The arrangement is different from the ADP-bound state of an analogously truncated, soluble FtsH construct from Thermotoga maritima. The pore is completely closed and the phenylalanine residues in the pore line a contiguous path. The protease hexamer is very similar to those described for other FtsH structures. To resolve certain open issues regarding a conserved glycine in the linker between the AAA and protease domains, as well as the active-site switch β-strand, mutations have been introduced in the full-length membrane-bound protein. Activity analysis of these point mutants reveals the crucial importance of these residues for proteolytic activity and is in accord with previous interpretation of the active-site switch and the importance of the linker glycine residue.
- Language
-
- English
- Open access status
- closed
- Identifiers
-
- DOI 10.1107/S1399004715005945
- PMID 26057670
- Persistent URL
- https://sonar.ch/global/documents/278533
Statistics
Document views: 18
File downloads: