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PROTEIN STRUCTURE REPORT

Crystal structure of the N-terminal domain of E. coli Lon protease

¹ Macromolecular Crystallography Laboratory, National Cancer Institute at Frederick, Frederick, Maryland 21702-1201, USA
² Basic Research Program, SAIC-Frederick, Frederick, Maryland 21702, USA
³ Laboratory of Cell Biology, National Cancer Institute, Bethesda, Maryland 20892, USA
⁴ Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow 117997, Russia

(RECEIVED July 28, 2005; FINAL REVISION July 28, 2005; ACCEPTED August 10, 2005)

We report here the first crystal structure of the N-terminal domain of an A-type Lon protease. Lon proteases are ubiquitous, multidomain, ATP-dependent enzymes with both highly specific and non-specific protein binding, unfolding, and degrading activities. We expressed and purified a stable, monomeric 119-amino acid N-terminal subdomain of the Escherichia coli A-type Lon protease and determined its crystal structure at 2.03 Å (Protein Data Bank [PDB] code 2ANE). The structure was solved in two crystal forms, yielding 14 independent views. The domain exhibits a unique fold consisting primarily of three twisted -sheets and a single long -helix. Analysis of recent PDB depositions identified a similar fold in BPP1347 (PDB code 1ZBO), a 203-amino acid protein of unknown function from Bordetella parapertussis, crystallized as part of a structural genomics effort. BPP1347 shares sequence homology with Lon N-domains and with a family of other independently expressed proteins of unknown functions. We postulate that, as is the case in Lon proteases, this structural domain represents a general protein and polypeptide interaction domain.

Keywords: ATP-dependent proteases; protein domain; structural genomics

Article published online ahead of print. Article and publication date are at http://www.proteinscience.org/cgi/doi/10.1110/ps.051736805.

Reprint requests to: Alexander Wlodawer, National Cancer Institute, MCL, Building 536, Room 5, Frederick, MD 21702-1201, USA; e-mail: wlodawer{at}ncifcrf.gov; fax: (301) 846-6128.

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