Hexameric Ring Structure of the ATPase Domain of the Membrane-Integrated Metalloprotease FtsH from Thermus thermophilus HB8
| Autor: | Hajime Niwa, Masasuke Yoshida, Hisayoshi Makyio, Daisuke Tsuchiya, Kosuke Morikawa |
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| Rok vydání: | 2002 |
| Předmět: |
Models
Molecular Conformational change metalloprotease Protein Conformation ATPase hexameric ring structure Molecular Sequence Data Protein structure Bacterial Proteins Structural Biology Amino Acid Sequence Binding site AAA ATPase Peptide sequence Molecular Biology DNA Primers FtsH Adenosine Triphosphatases substrate translocation Binding Sites Base Sequence Sequence Homology Amino Acid biology Nucleotides Thermus thermophilus Membrane Proteins biology.organism_classification AAA proteins Biochemistry Membrane protein Biophysics biology.protein |
| Zdroj: | Structure. 10(10):1415-1424 |
| ISSN: | 0969-2126 |
| DOI: | 10.1016/s0969-2126(02)00855-9 |
| Popis: | FtsH is a cytoplasmic membrane-integrated, ATP-dependent metalloprotease, which processively degrades both cytoplasmic and membrane proteins in concert with unfolding. The FtsH protein is divided into the N-terminal transmembrane region and the larger C-terminal cytoplasmic region, which consists of an ATPase domain and a protease domain. We have determined the crystal structures of the Thermus thermophilus FtsH ATPase domain in the nucleotide-free and AMP-PNP- and ADP-bound states, in addition to the domain with the extra preceding segment. Combined with the mapping of the putative substrate binding region, these structures suggest that FtsH internally forms a hexameric ring structure, in which ATP binding could cause a conformational change to facilitate transport of substrates into the protease domain through the central pore. |
| Databáze: | OpenAIRE |
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