3KDS
apo-FtsH crystal structure
Summary for 3KDS
| Entry DOI | 10.2210/pdb3kds/pdb |
| Related | 2CE7 2CEA |
| Descriptor | Cell division protein FtsH, ZINC ION, N-{(2R)-2-[2-(hydroxyamino)-2-oxoethyl]-4-methylpentanoyl}-3-naphthalen-2-yl-L-alanyl-L-alaninamide (3 entities in total) |
| Functional Keywords | met-turn, beta roll, metal binding protein |
| Biological source | Thermotoga maritima |
| Cellular location | Cell inner membrane; Multi-pass membrane protein; Cytoplasmic side (By similarity): Q9WZ49 |
| Total number of polymer chains | 3 |
| Total formula weight | 155807.65 |
| Authors | Bieniossek, C.,Niederhauser, B.,Baumann, U. (deposition date: 2009-10-23, release date: 2009-12-01, Last modification date: 2023-11-01) |
| Primary citation | Bieniossek, C.,Niederhauser, B.,Baumann, U.M. The crystal structure of apo-FtsH reveals domain movements necessary for substrate unfolding and translocation Proc.Natl.Acad.Sci.USA, 106:21579-21584, 2009 Cited by PubMed Abstract: The hexameric membrane-spanning ATP-dependent metalloprotease FtsH is universally conserved in eubacteria, mitochondria, and chloroplasts, where it fulfills key functions in quality control and signaling. As a member of the self-compartmentalizing ATPases associated with various cellular activities (AAA+ proteases), FtsH converts the chemical energy stored in ATP via conformational rearrangements into a mechanical force that is used for substrate unfolding and translocation into the proteolytic chamber. The crystal structure of the ADP state of Thermotoga maritima FtsH showed a hexameric assembly consisting of a 6-fold symmetric protease disk and a 2-fold symmetric AAA ring. The 2.6 A resolution structure of the cytosolic region of apo-FtsH presented here reveals a new arrangement where the ATPase ring shows perfect 6-fold symmetry with the crucial pore residues lining an open circular entrance. Triggered by this conformational change, a substrate-binding edge beta strand appears within the proteolytic domain. Comparison of the apo- and ADP-bound structure visualizes an inward movement of the aromatic pore residues and generates a model of substrate translocation by AAA+ proteases. Furthermore, we demonstrate that mutation of a conserved glycine in the linker region inactivates FtsH. PubMed: 19955424DOI: 10.1073/pnas.0910708106 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.601 Å) |
Structure validation
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