1n61
From Proteopedia
(New page: 200px<br /><applet load="1n61" size="450" color="white" frame="true" align="right" spinBox="true" caption="1n61, resolution 1.3Å" /> '''Crystal Structure of ...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1n61.gif|left|200px]]<br /><applet load="1n61" size=" | + | [[Image:1n61.gif|left|200px]]<br /><applet load="1n61" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1n61, resolution 1.3Å" /> | caption="1n61, resolution 1.3Å" /> | ||
'''Crystal Structure of the Cu,Mo-CO Dehydrogenase (CODH); Dithionite reduced state'''<br /> | '''Crystal Structure of the Cu,Mo-CO Dehydrogenase (CODH); Dithionite reduced state'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The CO dehydrogenase of the eubacterium Oligotropha carboxidovorans is a | + | The CO dehydrogenase of the eubacterium Oligotropha carboxidovorans is a 277-kDa Mo- and Cu-containing iron-sulfur flavoprotein. Here, the enzyme's active site in the oxidized or reduced state, after inactivation with potassium cyanide or with n-butylisocyanide bound to the active site, has been reinvestigated by multiple wavelength anomalous dispersion measurements at atomic resolution, electron spin resonance spectroscopy, and chemical analyses. We present evidence for a dinuclear heterometal [CuSMoO)OH] cluster in the active site of the oxidized or reduced enzyme, which is prone to cyanolysis. The cluster is coordinated through interactions of the Mo with the dithiolate pyran ring of molybdopterin cytosine dinucleotide and of the Cu with the Sgamma of Cys-388, which is part of the active-site loop VAYRC(388)SFR. The previously reported active-site structure [Dobbek, H., Gremer, L., Meyer, O. & Huber, R. (1999) Proc. Natl. Acad. Sci. USA 96, 8884-8889] of an Mo with three oxygen ligands and an SeH-group bound to the Sgamma atom of Cys-388 could not be confirmed. The structure of CO dehydrogenase with the inhibitor n-butylisocyanide bound has led to a model for the catalytic mechanism of CO oxidation which involves a thiocarbonate-like intermediate state. The dinuclear [CuSMo(O)OH] cluster of CO dehydrogenase establishes a previously uncharacterized class of dinuclear molybdoenzymes containing the pterin cofactor. |
==About this Structure== | ==About this Structure== | ||
| - | 1N61 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Oligotropha_carboxidovorans Oligotropha carboxidovorans] with PO4, FES, CUN, MCN and FAD as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Carbon-monoxide_dehydrogenase_(acceptor) Carbon-monoxide dehydrogenase (acceptor)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.2.99.2 1.2.99.2] Full crystallographic information is available from [http:// | + | 1N61 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Oligotropha_carboxidovorans Oligotropha carboxidovorans] with <scene name='pdbligand=PO4:'>PO4</scene>, <scene name='pdbligand=FES:'>FES</scene>, <scene name='pdbligand=CUN:'>CUN</scene>, <scene name='pdbligand=MCN:'>MCN</scene> and <scene name='pdbligand=FAD:'>FAD</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Carbon-monoxide_dehydrogenase_(acceptor) Carbon-monoxide dehydrogenase (acceptor)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.2.99.2 1.2.99.2] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N61 OCA]. |
==Reference== | ==Reference== | ||
| Line 29: | Line 29: | ||
[[Category: molybdopterin]] | [[Category: molybdopterin]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:02:41 2008'' |
Revision as of 12:02, 21 February 2008
|
Crystal Structure of the Cu,Mo-CO Dehydrogenase (CODH); Dithionite reduced state
Overview
The CO dehydrogenase of the eubacterium Oligotropha carboxidovorans is a 277-kDa Mo- and Cu-containing iron-sulfur flavoprotein. Here, the enzyme's active site in the oxidized or reduced state, after inactivation with potassium cyanide or with n-butylisocyanide bound to the active site, has been reinvestigated by multiple wavelength anomalous dispersion measurements at atomic resolution, electron spin resonance spectroscopy, and chemical analyses. We present evidence for a dinuclear heterometal [CuSMoO)OH] cluster in the active site of the oxidized or reduced enzyme, which is prone to cyanolysis. The cluster is coordinated through interactions of the Mo with the dithiolate pyran ring of molybdopterin cytosine dinucleotide and of the Cu with the Sgamma of Cys-388, which is part of the active-site loop VAYRC(388)SFR. The previously reported active-site structure [Dobbek, H., Gremer, L., Meyer, O. & Huber, R. (1999) Proc. Natl. Acad. Sci. USA 96, 8884-8889] of an Mo with three oxygen ligands and an SeH-group bound to the Sgamma atom of Cys-388 could not be confirmed. The structure of CO dehydrogenase with the inhibitor n-butylisocyanide bound has led to a model for the catalytic mechanism of CO oxidation which involves a thiocarbonate-like intermediate state. The dinuclear [CuSMo(O)OH] cluster of CO dehydrogenase establishes a previously uncharacterized class of dinuclear molybdoenzymes containing the pterin cofactor.
About this Structure
1N61 is a Protein complex structure of sequences from Oligotropha carboxidovorans with , , , and as ligands. Active as Carbon-monoxide dehydrogenase (acceptor), with EC number 1.2.99.2 Full crystallographic information is available from OCA.
Reference
Catalysis at a dinuclear [CuSMo(==O)OH] cluster in a CO dehydrogenase resolved at 1.1-A resolution., Dobbek H, Gremer L, Kiefersauer R, Huber R, Meyer O, Proc Natl Acad Sci U S A. 2002 Dec 10;99(25):15971-6. PMID:12475995
Page seeded by OCA on Thu Feb 21 14:02:41 2008
Categories: Carbon-monoxide dehydrogenase (acceptor) | Oligotropha carboxidovorans | Protein complex | Dobbek, H. | Gremer, L. | Huber, R. | Kiefersauer, R. | Meyer, O. | CUN | FAD | FES | MCN | PO4 | Codh | Copper | Molybdenum | Molybdopterin
