1IY1

Crystal structure of the FtsH ATPase domain with ADP from Thermus thermophilus

Summary for 1IY1

• Entry DOI: 10.2210/pdb1iy1/pdb
• Related: 1IXZ 1IY0 1IY2
• Descriptor: ATP-dependent metalloprotease FtsH, ADENOSINE-5'-DIPHOSPHATE (3 entities in total)
• Functional Keywords: aaa domain fold, hydrolase
• Biological source: Thermus thermophilus
• Total number of polymer chains: 1
• Total formula weight: 27812.66

Authors

Niwa, H.,Tsuchiya, D.,Makyio, H.,Yoshida, M.,Morikawa, K. (deposition date: 2002-07-10, release date: 2002-11-06, Last modification date: 2023-12-27)

Primary citation

Niwa, H.,Tsuchiya, D.,Makyio, H.,Yoshida, M.,Morikawa, K.
Hexameric ring structure of the ATPase domain of the membrane-integrated metalloprotease FtsH from Thermus thermophilus HB8
Structure, 10:1415-1423, 2002

PubMed Abstract: 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.

PubMed: 12377127
DOI: 10.1016/S0969-2126(02)00855-9

Experimental method

X-RAY DIFFRACTION (2.8 Å)