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PMID:15037242
| Citation |
Botos, I, Melnikov, EE, Cherry, S, Khalatova, AG, Rasulova, FS, Tropea, JE, Maurizi, MR, Rotanova, TV, Gustchina, A and Wlodawer, A Crystal structure of the AAA+ alpha domain of E. coli Lon protease at 1.9A resolution. J. Struct. Biol. 146:113-22 |
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| 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. |
| Links |
PubMed Online version:10.1016/j.jsb.2003.09.003 |
| Keywords |
Adenosine Triphosphatases/chemistry; Arginine; Crystallography, X-Ray/methods; Escherichia coli Proteins/chemistry; Molecular Structure; Peptide Fragments/chemistry; Protease La/chemistry; Protein Structure, Tertiary |
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Significance
Annotations
| Gene product | Qualifier | GO ID | GO term name | Evidence Code | with/from | Aspect | Notes | Status |
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