1QZM

alpha-domain of ATPase

Summary for 1QZM

• Entry DOI: 10.2210/pdb1qzm/pdb
• Descriptor: ATP-dependent protease La (2 entities in total)
• Functional Keywords: oligomerization domain, aaa+ protein, atp-dependent protease, hydrolase
• Biological source: Escherichia coli
• Cellular location: Cytoplasm: P0A9M0
• Total number of polymer chains: 1
• Total formula weight: 10838.53

Authors

Botos, I.,Melnikov, E.E.,Cherry, S.,Khalatova, A.G.,Rasulova, F.S.,Tropea, J.E.,Maurizi, M.R.,Rotanova, T.V.,Gustchina, A.,Wlodawer, A. (deposition date: 2003-09-17, release date: 2004-05-04, Last modification date: 2024-02-14)

Primary citation

Botos, I.,Melnikov, E.E.,Cherry, S.,Khalatova, A.G.,Rasulova, F.S.,Tropea, J.E.,Maurizi, M.R.,Rotanova, T.V.,Gustchina, A.,Wlodawer, A.
Crystal structure of the AAA+ alpha domain of E. coli Lon protease at 1.9A resolution.
J.Struct.Biol., 146:113-122,

PubMed Abstract: The crystal structure of the small, mostly helical alpha domain of the AAA+ module of the Escherichia coli ATP-dependent protease Lon has been solved by single isomorphous replacement combined with anomalous scattering and refined at 1.9A resolution to a crystallographic R factor of 17.9%. This domain, comprising residues 491-584, was obtained by chymotrypsin digestion of the recombinant full-length protease. The alpha domain of Lon contains four alpha helices and two parallel strands and resembles similar domains found in a variety of ATPases and helicases, including the oligomeric proteases HslVU and ClpAP. The highly conserved "sensor-2" Arg residue is located at the beginning of the third helix. Detailed comparison with the structures of 11 similar domains established the putative location of the nucleotide-binding site in this first fragment of Lon for which a crystal structure has become available.

PubMed: 15037242
DOI: 10.1016/j.jsb.2003.09.003

Experimental method

X-RAY DIFFRACTION (1.9 Å)