| Literature DB >> 15037242 |
Istvan Botos1, Edward E Melnikov, Scott Cherry, Anna G Khalatova, Fatima S Rasulova, Joseph E Tropea, Michael R Maurizi, Tatyana V Rotanova, Alla Gustchina, Alexander Wlodawer.
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.Entities:
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Year: 2004 PMID： 15037242 DOI： 10.1016/j.jsb.2003.09.003
Source DB: PubMed Journal: J Struct Biol ISSN： 1047-8477 Impact factor: 2.867