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Crystal structure of the AAA(+) alpha domain of E-coli Lon protease at 1.9 angstrom resolution

  1. Author:
    Botos, I.
    Melnikov, E. E.
    Cherry, S.
    Khalatova, A. G.
    Rasulova, F. S.
    Tropea, J. E.
    Maurizi, M. R.
    Rotanova, T. V.
    Gustchina, A.
    Wlodawer, A.

  2. Author Address

    Wlodawer, A, NCI, Ctr Macromol Crystallog, MCL Bldg 536,Rm 5, Frederick, MD 21702 USA NCI, Ctr Macromol Crystallog, Frederick, MD 21702 USA. Russian Acad Sci, Shemyakin Ovchinnikov Inst Bioorgan Chem, Moscow 117997, Russia. NCI, Cell Biol Lab, Bethesda, MD 20892 USA.
    1. Year: 2004
    2. Date: APR-MAY
  2. Journal: Journal of Structural Biology
    1. 146
    2. 1-2
    3. Pages: 113-122
  4. Type of Article: Article
  1. 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 1.9 Angstrom 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 Hs1VU 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. (C) 2003 Elsevier Inc. All rights reserved

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