2ANE

Crystal structure of N-terminal domain of E.Coli Lon Protease

Summary for 2ANE

• Entry DOI: 10.2210/pdb2ane/pdb
• Descriptor: ATP-dependent protease La (2 entities in total)
• Functional Keywords: lonn119, lon protease, hydrolase
• Biological source: Escherichia coli
• Cellular location: Cytoplasm: P0A9M0
• Total number of polymer chains: 8
• Total formula weight: 112834.62

Authors

Li, M.,Rasulova, F.,Melnikov, E.E.,Rotanova, T.V.,Gustchina, A.,Maurizi, M.R.,Wlodawer, A. (deposition date: 2005-08-11, release date: 2005-11-01, Last modification date: 2024-02-14)

Primary citation

Li, M.,Rasulova, F.,Melnikov, E.E.,Rotanova, T.V.,Gustchina, A.,Maurizi, M.R.,Wlodawer, A.
Crystal structure of the N-terminal domain of E. coli Lon protease.
Protein Sci., 14:2895-2900, 2005

PubMed 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.

PubMed: 16199667
DOI: 10.1110/ps.051736805

Experimental method

X-RAY DIFFRACTION (2.03 Å)