| Autor: |
Botos I; Macromolecular Crystallography Laboratory, National Cancer Institute at Frederick, MCL Bldg. 536, Rm. 5, Frederick, MD 21702-1201, USA., Melnikov EE, Cherry S, Khalatova AG, Rasulova FS, Tropea JE, Maurizi MR, Rotanova TV, Gustchina A, Wlodawer A |
| Jazyk: |
angličtina |
| Zdroj: |
Journal of structural biology [J Struct Biol] 2004 Apr-May; Vol. 146 (1-2), pp. 113-22. |
| DOI: |
10.1016/j.jsb.2003.09.003 |
| Abstrakt: |
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. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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