1QZM: Alpha-domain Of Atpase

Citation:
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.
PDB ID: 1QZMDownload
MMDB ID: 27293
PDB Deposition Date: 2003/9/17
Updated in MMDB: 2017/11
Experimental Method:
x-ray diffraction
Resolution: 1.9  Å
Source Organism:
Similar Structures:
Biological Unit for 1QZM: monomeric; determined by author
Molecular Components in 1QZM
Label Count Molecule
Protein (1 molecule)
1
Atp-dependent Protease LA(Gene symbol: lon)
Molecule annotation
* Click molecule labels to explore molecular sequence information.

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