2ane
From Proteopedia
(New page: 200px<br /><applet load="2ane" size="450" color="white" frame="true" align="right" spinBox="true" caption="2ane, resolution 2.03Å" /> '''Crystal structure of...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:2ane.gif|left|200px]]<br /><applet load="2ane" size=" | + | [[Image:2ane.gif|left|200px]]<br /><applet load="2ane" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2ane, resolution 2.03Å" /> | caption="2ane, resolution 2.03Å" /> | ||
'''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== | ||
| - | We report here the first crystal structure of the N-terminal domain of an | + | 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== | ||
| - | 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:// | + | 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== | ||
| Line 16: | Line 16: | ||
[[Category: Gustchina, A.]] | [[Category: Gustchina, A.]] | ||
[[Category: Li, M.]] | [[Category: Li, M.]] | ||
| - | [[Category: Maurizi, M | + | [[Category: Maurizi, M R.]] |
| - | [[Category: Melnikov, E | + | [[Category: Melnikov, E E.]] |
[[Category: Rasulova, F.]] | [[Category: Rasulova, F.]] | ||
| - | [[Category: Rotanova, T | + | [[Category: Rotanova, T V.]] |
[[Category: Wlodawer, A.]] | [[Category: Wlodawer, A.]] | ||
[[Category: lon protease]] | [[Category: lon protease]] | ||
[[Category: lonn119]] | [[Category: lonn119]] | ||
| - | ''Page seeded by [http:// | + | ''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
|
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
Page seeded by OCA on Thu Feb 21 16:29:04 2008
