2azq
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(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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Revision as of 16:13, 29 January 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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