Crystal structure of the N-terminal domain of E. coli Lon protease |
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Authors: | Li Mi Rasulova Fatima Melnikov Edward E Rotanova Tatyana V Gustchina Alla Maurizi Michael R Wlodawer Alexander |
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Institution: | Macromolecular Crystallography Laboratory, National Cancer Institute, Building 536, Room 5, Frederick, MD 21702-1201, USA. |
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Abstract: | 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 A (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 beta-sheets and a single long alpha-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. |
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Keywords: | ATP-dependent proteases protein domain structural genomics |
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