2ane

From Proteopedia

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

Overview

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.

About this Structure

2ANE is a Single protein structure of sequence from Escherichia coli. Active as Endopeptidase La, with EC number 3.4.21.53 Full crystallographic information is available from OCA.

Reference

Crystal structure of the N-terminal domain of E. coli Lon protease., Li M, Rasulova F, Melnikov EE, Rotanova TV, Gustchina A, Maurizi MR, Wlodawer A, Protein Sci. 2005 Nov;14(11):2895-900. Epub 2005 Sep 30. PMID:16199667

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