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458 a.a.
Key reference
DOI no: 10.1016/j.molcel.2006.04.020 Mol Cell 22:575-585 (2006) PubMed id: 16762831
Structure of the whole cytosolic region of ATP-dependent protease FtsH. R.Suno, H.Niwa, D.Tsuchiya, X.Zhang, M.Yoshida, K.Morikawa. ABSTRACT
An ATP-dependent protease, FtsH, digests misassembled membrane proteins in order to maintain membrane integrity and digests short-lived soluble proteins in order to control their cellular regulation. This enzyme has an N-terminal transmembrane segment and a C-terminal cytosolic region consisting of an AAA+ ATPase domain and a protease domain. Here we present two crystal structures: the protease domain and the whole cytosolic region. The cytosolic region fully retains an ATP-dependent protease activity and adopts a three-fold-symmetric hexameric structure. The protease domains displayed a six-fold symmetry, while the AAA+ domains, each containing ADP, alternate two orientations relative to the protease domain, making "open" and "closed" interdomain contacts. Apparently, ATPase is active only in the closed form, and protease operates in the open form. The protease catalytic sites are accessible only through a tunnel following from the AAA+ domain of the adjacent subunit, raising a possibility of translocation of polypeptide substrate to the protease sites through this tunnel.
Selected figure(s)
Figure 4.
Figure 4. Catalytic Environments in sFtsHFigure 6.
Figure 6. The ATPase Cycle and Putative Polypeptide Translocation PathwayThe above figures are reprinted by permission from Cell Press: Mol Cell (2006, 22, 575-585) copyright 2006. Figures were selected by the author.
Literature references that cite this PDB file's key reference
PubMed id Reference
19332814 A.T.Le, and W.Schumann (2009).
The Spo0E phosphatase of Bacillus subtilis is a substrate of the FtsH metalloprotease.Microbiology, 155, 1122-1132.
19841671 T.Karlberg, S.van den Berg, M.Hammarström, J.Sagemark, I.Johansson, L.Holmberg-Schiavone, and H.Schüler (2009).
Crystal structure of the ATPase domain of the human AAA+ protein paraplegin/SPG7.PLoS One, 4, e6975.
PDB code: 2qz4
18466635 J.Snider, G.Thibault, and W.A.Houry (2008).
The AAA+ superfamily of functionally diverse proteins.Genome Biol, 9, 216.
18421140 S.H.Kim, G.B.Kang, H.E.Song, S.J.Park, M.H.Bea, and S.H.Eom (2008).
Structural studies on Helicobacter pyloriATP-dependent protease, FtsH.J Synchrotron Radiat, 15, 208-210.
PDB codes: 2r62 2r65
18670904 S.I.Allakhverdiev, and N.Murata (2008).
Salt stress inhibits photosystems II and I in cyanobacteria.Photosynth Res, 98, 529-539.
19011636 T.Masaike, F.Koyama-Horibe, K.Oiwa, M.Yoshida, and T.Nishizaka (2008).
Cooperative three-step motions in catalytic subunits of F(1)-ATPase correlate with 80 degrees and 40 degrees substep rotations.Nat Struct Mol Biol, 15, 1326-1333.
17242399 J.Schumacher, N.Joly, M.Rappas, D.Bradley, S.R.Wigneshweraraj, X.Zhang, and M.Buck (2007).
Sensor I threonine of the AAA+ ATPase transcriptional activator PspF is involved in coupling nucleotide triphosphate hydrolysis to the restructuring of sigma 54-RNA polymerase.J Biol Chem, 282, 9825-9833.
17261594 M.Graef, G.Seewald, and T.Langer (2007).
Substrate recognition by AAA+ ATPases: distinct substrate binding modes in ATP-dependent protease Yme1 of the mitochondrial intermembrane space.Mol Cell Biol, 27, 2476-2485.
17101804 M.Koppen, M.D.Metodiev, G.Casari, E.I.Rugarli, and T.Langer (2007).
Variable and tissue-specific subunit composition of mitochondrial m-AAA protease complexes linked to hereditary spastic paraplegia.Mol Cell Biol, 27, 758-767.
17245427 T.Tatsuta, S.Augustin, M.Nolden, B.Friedrichs, and T.Langer (2007).
m-AAA protease-driven membrane dislocation allows intramembrane cleavage by rhomboid in mitochondria.EMBO J, 26, 325-335. The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB code is shown on the right.
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