Universität zu Köln

Vostrukhina, Marina, Popov, Alexander ORCID: 0000-0002-3058-8912, Brunstein, Elena, Lanz, Martin A., Baumgartner, Renato, Bieniossek, Christoph, Schacherl, Magdalena ORCID: 0000-0002-5478-2509 and Baumann, Ulrich (2015). The structure of Aquifex aeolicus FtsH in the ADP-bound state reveals a C-2-symmetric hexamer. Acta Crystallogr. Sect. D-Struct. Biol., 71. S. 1307 - 1319. CHESTER: INT UNION CRYSTALLOGRAPHY. ISSN 2059-7983

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Abstract

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 angstrom 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 beta-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.

Item Type:	Journal Article
Creators:	Creators Email ORCID ORCID Put Code Vostrukhina, Marina UNSPECIFIED UNSPECIFIED UNSPECIFIED Popov, Alexander UNSPECIFIED orcid.org/0000-0002-3058-8912 UNSPECIFIED Brunstein, Elena UNSPECIFIED UNSPECIFIED UNSPECIFIED Lanz, Martin A. UNSPECIFIED UNSPECIFIED UNSPECIFIED Baumgartner, Renato UNSPECIFIED UNSPECIFIED UNSPECIFIED Bieniossek, Christoph UNSPECIFIED UNSPECIFIED UNSPECIFIED Schacherl, Magdalena UNSPECIFIED orcid.org/0000-0002-5478-2509 UNSPECIFIED Baumann, Ulrich UNSPECIFIED UNSPECIFIED UNSPECIFIED
URN:	urn:nbn:de:hbz:38-402595
DOI:	10.1107/S1399004715005945
Journal or Publication Title:	Acta Crystallogr. Sect. D-Struct. Biol.
Volume:	71
Page Range:	S. 1307 - 1319
Date:	2015
Publisher:	INT UNION CRYSTALLOGRAPHY
Place of Publication:	CHESTER
ISSN:	2059-7983
Language:	English
Faculty:	Faculty of Mathematics and Natural Sciences
Divisions:	Faculty of Mathematics and Natural Sciences > Department of Chemistry > Institute of Biochemistry
Subjects:	no entry
Uncontrolled Keywords:	Keywords Language ATP-FUELED MACHINES; AAA PROTEASE FTSH; MACROMOLECULAR STRUCTURES; MAXIMUM-LIKELIHOOD; ATOMIC STRUCTURES; REFINEMENT; PROTEINS; CRYSTALLOGRAPHY; ARCHITECTURE; INFORMATION Multiple languages Biochemical Research Methods; Biochemistry & Molecular Biology; Biophysics; Crystallography Multiple languages
Refereed:	Yes
URI:	http://kups.ub.uni-koeln.de/id/eprint/40259