1wql
From Proteopedia
(New page: 200px<br /><applet load="1wql" size="450" color="white" frame="true" align="right" spinBox="true" caption="1wql, resolution 2.20Å" /> '''Cumene dioxygenase (...) |
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| - | [[Image:1wql.gif|left|200px]]<br /><applet load="1wql" size=" | + | [[Image:1wql.gif|left|200px]]<br /><applet load="1wql" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1wql, resolution 2.20Å" /> | caption="1wql, resolution 2.20Å" /> | ||
'''Cumene dioxygenase (cumA1A2) from Pseudomonas fluorescens IP01'''<br /> | '''Cumene dioxygenase (cumA1A2) from Pseudomonas fluorescens IP01'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The crystal structure of the terminal component of the cumene dioxygenase | + | The crystal structure of the terminal component of the cumene dioxygenase multicomponent enzyme system of Pseudomonas fluorescens IP01 (CumDO) was determined at a resolution of 2.2 A by means of molecular replacement by using the crystal structure of the terminal oxygenase component of naphthalene dioxygenase from Pseudomonas sp. strain NCIB 9816-4 (NphDO). The ligation of the two catalytic centers of CumDO (i.e., the nonheme iron and Rieske [2Fe-2S] centers) and the bridging between them in neighboring catalytic subunits by hydrogen bonds through a single amino acid residue, Asp231, are similar to those of NphDO. An unidentified external ligand, possibly dioxygen, was bound at the active site nonheme iron. The entrance to the active site of CumDO is different from the entrance to the active site of NphDO, as the two loops forming the lid exhibit great deviation. On the basis of the complex structure of NphDO, a biphenyl substrate was modeled in the substrate-binding pocket of CumDO. The residues surrounding the modeled biphenyl molecule include residues that have already been shown to be important for its substrate specificity by a number of engineering studies of biphenyl dioxygenases. |
==About this Structure== | ==About this Structure== | ||
| - | 1WQL is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Pseudomonas_fluorescens Pseudomonas fluorescens] with FE2, FES and OXY as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1WQL is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Pseudomonas_fluorescens Pseudomonas fluorescens] with <scene name='pdbligand=FE2:'>FE2</scene>, <scene name='pdbligand=FES:'>FES</scene> and <scene name='pdbligand=OXY:'>OXY</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WQL OCA]. |
==Reference== | ==Reference== | ||
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[[Category: rieske non-heme iron dioxygenase]] | [[Category: rieske non-heme iron dioxygenase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:47:13 2008'' |
Revision as of 13:47, 21 February 2008
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Cumene dioxygenase (cumA1A2) from Pseudomonas fluorescens IP01
Overview
The crystal structure of the terminal component of the cumene dioxygenase multicomponent enzyme system of Pseudomonas fluorescens IP01 (CumDO) was determined at a resolution of 2.2 A by means of molecular replacement by using the crystal structure of the terminal oxygenase component of naphthalene dioxygenase from Pseudomonas sp. strain NCIB 9816-4 (NphDO). The ligation of the two catalytic centers of CumDO (i.e., the nonheme iron and Rieske [2Fe-2S] centers) and the bridging between them in neighboring catalytic subunits by hydrogen bonds through a single amino acid residue, Asp231, are similar to those of NphDO. An unidentified external ligand, possibly dioxygen, was bound at the active site nonheme iron. The entrance to the active site of CumDO is different from the entrance to the active site of NphDO, as the two loops forming the lid exhibit great deviation. On the basis of the complex structure of NphDO, a biphenyl substrate was modeled in the substrate-binding pocket of CumDO. The residues surrounding the modeled biphenyl molecule include residues that have already been shown to be important for its substrate specificity by a number of engineering studies of biphenyl dioxygenases.
About this Structure
1WQL is a Protein complex structure of sequences from Pseudomonas fluorescens with , and as ligands. Full crystallographic information is available from OCA.
Reference
Crystal structure of the terminal oxygenase component of cumene dioxygenase from Pseudomonas fluorescens IP01., Dong X, Fushinobu S, Fukuda E, Terada T, Nakamura S, Shimizu K, Nojiri H, Omori T, Shoun H, Wakagi T, J Bacteriol. 2005 Apr;187(7):2483-90. PMID:15774891
Page seeded by OCA on Thu Feb 21 15:47:13 2008
Categories: Protein complex | Pseudomonas fluorescens | Dong, X. | Fukuda, E. | Fushinobu, S. | Nakamura, S. | Nojiri, H. | Omori, T. | Shimizu, K. | Shoun, H. | Terada, T. | Wakagi, T. | FE2 | FES | OXY | Biphenyl dioxygenase | Cumene dioxygenase | Naphthalene dioxygenase | Polychlorinated biphenyl degradation | Rieske non-heme iron dioxygenase
