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2ane

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(New page: 200px<br /><applet load="2ane" size="450" color="white" frame="true" align="right" spinBox="true" caption="2ane, resolution 2.03&Aring;" /> '''Crystal structure of...)
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[[Image:2ane.gif|left|200px]]<br /><applet load="2ane" size="350" color="white" frame="true" align="right" spinBox="true"
caption="2ane, resolution 2.03&Aring;" />
caption="2ane, resolution 2.03&Aring;" />
'''Crystal structure of N-terminal domain of E.Coli Lon Protease'''<br />
'''Crystal structure of N-terminal domain of E.Coli Lon Protease'''<br />
==Overview==
==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.
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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.
==About this Structure==
==About this Structure==
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2ANE is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Active as [http://en.wikipedia.org/wiki/Endopeptidase_La Endopeptidase La], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.53 3.4.21.53] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2ANE OCA].
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2ANE is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Active as [http://en.wikipedia.org/wiki/Endopeptidase_La Endopeptidase La], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.53 3.4.21.53] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ANE OCA].
==Reference==
==Reference==
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[[Category: Gustchina, A.]]
[[Category: Gustchina, A.]]
[[Category: Li, M.]]
[[Category: Li, M.]]
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[[Category: Maurizi, M.R.]]
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[[Category: Maurizi, M R.]]
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[[Category: Melnikov, E.E.]]
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[[Category: Melnikov, E E.]]
[[Category: Rasulova, F.]]
[[Category: Rasulova, F.]]
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[[Category: Rotanova, T.V.]]
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[[Category: Rotanova, T V.]]
[[Category: Wlodawer, A.]]
[[Category: Wlodawer, A.]]
[[Category: lon protease]]
[[Category: lon protease]]
[[Category: lonn119]]
[[Category: lonn119]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 08:14:29 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:29:04 2008''

Revision as of 14:29, 21 February 2008


2ane, resolution 2.03Å

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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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