2azq
From Proteopedia
(New page: 200px<br /><applet load="2azq" size="350" color="white" frame="true" align="right" spinBox="true" caption="2azq, resolution 2.650Å" /> '''Crystal Structure o...) |
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==Overview== | ==Overview== | ||
| - | Catechol 1,2-dioxygenase was first studied by Hayaishi and colleagues in | + | Catechol 1,2-dioxygenase was first studied by Hayaishi and colleagues in 1950. In 1967, catechol 1,2-dioxygenase from Pseudomonas arvilla C-1 (PaCTD) was chosen as a model system for the catecholic intradiol dioxygenases due to its activity, stability and expression level. Here we report the 2.65 A structure of the betabeta isozyme of PaCTD. The structure supports the hypothesis first made by Vetting and Ohlendorf [The 1.8A crystal structure of catechol 1,2-dioxygenase reveals a novel hydrophobic helical zipper as a subunit linker, Struct. Fold. Des. 8 (2000) 429-440.] that the catechol 1,2-dioxygenases are lipid binding proteins. The 5 amino-terminal helices involved in dimerization and forming the lipid binding site are shown to be plastic in their positions and orientations. The sequence differences between the alpha and beta polypeptides are located at the part of the monomers distant from dimerization surface and thus permit the formation of the 3 isozymes (alphaalpha, alphabeta, and betabeta) of PaCTD. The reported inactivation by sulfhydryl-modifying reagents is explained by the structure. The 10-residue Helix F (residues 203-212) is proposed to be central in communicating between the lipid binding site and the active site. |
==About this Structure== | ==About this Structure== | ||
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[[Category: Pseudomonas putida]] | [[Category: Pseudomonas putida]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Earhart, C | + | [[Category: Earhart, C A.]] |
[[Category: Gosu, R.]] | [[Category: Gosu, R.]] | ||
[[Category: Michaud-Soret, I.]] | [[Category: Michaud-Soret, I.]] | ||
| - | [[Category: Ohlendorf, D | + | [[Category: Ohlendorf, D H.]] |
[[Category: Que, L.]] | [[Category: Que, L.]] | ||
| - | [[Category: Vetting, M | + | [[Category: Vetting, M W.]] |
[[Category: FE]] | [[Category: FE]] | ||
[[Category: PCF]] | [[Category: PCF]] | ||
[[Category: ctd; catechol; dioxygenase; lipid; isozyme; intradiol]] | [[Category: ctd; catechol; dioxygenase; lipid; isozyme; intradiol]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:32:41 2008'' |
Revision as of 14:32, 21 February 2008
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Crystal Structure of Catechol 1,2-Dioxygenase from Pseudomonas arvilla C-1
Overview
Catechol 1,2-dioxygenase was first studied by Hayaishi and colleagues in 1950. In 1967, catechol 1,2-dioxygenase from Pseudomonas arvilla C-1 (PaCTD) was chosen as a model system for the catecholic intradiol dioxygenases due to its activity, stability and expression level. Here we report the 2.65 A structure of the betabeta isozyme of PaCTD. The structure supports the hypothesis first made by Vetting and Ohlendorf [The 1.8A crystal structure of catechol 1,2-dioxygenase reveals a novel hydrophobic helical zipper as a subunit linker, Struct. Fold. Des. 8 (2000) 429-440.] that the catechol 1,2-dioxygenases are lipid binding proteins. The 5 amino-terminal helices involved in dimerization and forming the lipid binding site are shown to be plastic in their positions and orientations. The sequence differences between the alpha and beta polypeptides are located at the part of the monomers distant from dimerization surface and thus permit the formation of the 3 isozymes (alphaalpha, alphabeta, and betabeta) of PaCTD. The reported inactivation by sulfhydryl-modifying reagents is explained by the structure. The 10-residue Helix F (residues 203-212) is proposed to be central in communicating between the lipid binding site and the active site.
About this Structure
2AZQ is a Single protein structure of sequence from Pseudomonas putida with and as ligands. Active as Catechol 1,2-dioxygenase, with EC number 1.13.11.1 Full crystallographic information is available from OCA.
Reference
Structure of catechol 1,2-dioxygenase from Pseudomonas arvilla., Earhart CA, Vetting MW, Gosu R, Michaud-Soret I, Que L Jr, Ohlendorf DH, Biochem Biophys Res Commun. 2005 Dec 9;338(1):198-205. Epub 2005 Sep 8. PMID:16171781
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