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| {{STRUCTURE_2ane| PDB=2ane | SCENE= }} | | {{STRUCTURE_2ane| PDB=2ane | SCENE= }} |
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| '''Crystal structure of N-terminal domain of E.Coli Lon Protease'''
| | ===Crystal structure of N-terminal domain of E.Coli Lon Protease=== |
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| ==Overview==
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| 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.
| | The line below this paragraph, {{ABSTRACT_PUBMED_16199667}}, adds the Publication Abstract to the page |
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| | {{ABSTRACT_PUBMED_16199667}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Lon protease]] | | [[Category: Lon protease]] |
| [[Category: Lonn119]] | | [[Category: Lonn119]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 19:15:05 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 11:11:53 2008'' |
