Crystal structure of the AAA+ alpha domain of E. coli Lon protease at 1.9A resolution.
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.
Botos
Istvan
I
Macromolecular Crystallography Laboratory, National Cancer Institute at Frederick, MCL Bldg. 536, Rm. 5, Frederick, MD 21702-1201, USA.
Melnikov
Edward E
EE
Cherry
Scott
S
Khalatova
Anna G
AG
Rasulova
Fatima S
FS
Tropea
Joseph E
JE
Maurizi
Michael R
MR
Rotanova
Tatyana V
TV
Gustchina
Alla
A
Wlodawer
Alexander
A
D000251:Adenosine Triphosphatases / Q000737:chemistry; D001120:Arginine; D018360:Crystallography, X-Ray / Q000379:methods; D029968:Escherichia coli Proteins / Q000737:chemistry*; D015394:Molecular Structure; D010446:Peptide Fragments / Q000737:chemistry; D049070:Protease La / Q000737:chemistry*; D017434:Protein Structure, Tertiary
D029968:Escherichia coli Proteins; D010446:Peptide Fragments; D001120:Arginine; C483567:Lon protein, E coli; D049070:Protease La; D000251:Adenosine Triphosphatases