1krh
From Proteopedia
(New page: 200px<br /><applet load="1krh" size="450" color="white" frame="true" align="right" spinBox="true" caption="1krh, resolution 1.5Å" /> '''X-ray Stucture of Ben...) |
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| - | [[Image:1krh.jpg|left|200px]]<br /><applet load="1krh" size=" | + | [[Image:1krh.jpg|left|200px]]<br /><applet load="1krh" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1krh, resolution 1.5Å" /> | caption="1krh, resolution 1.5Å" /> | ||
'''X-ray Stucture of Benzoate Dioxygenase Reductase'''<br /> | '''X-ray Stucture of Benzoate Dioxygenase Reductase'''<br /> | ||
==Overview== | ==Overview== | ||
| - | One of the major processes for aerobic biodegradation of aromatic | + | One of the major processes for aerobic biodegradation of aromatic compounds is initiated by Rieske dioxygenases. Benzoate dioxygenase contains a reductase component, BenC, that is responsible for the two-electron transfer from NADH via FAD and an iron-sulfur cluster to the terminal oxygenase component. Here, we present the structure of BenC from Acinetobacter sp. strain ADP1 at 1.5 A resolution. BenC contains three domains, each binding a redox cofactor: iron-sulfur, FAD and NADH, respectively. The [2Fe-2S] domain is similar to that of plant ferredoxins, and the FAD and NADH domains are similar to members of the ferredoxin:NADPH reductase superfamily. In phthalate dioxygenase reductase, the only other Rieske dioxygenase reductase for which a crystal structure is available, the ferredoxin-like and flavin binding domains are sequentially reversed compared to BenC. The BenC structure shows significant differences in the location of the ferredoxin domain relative to the other domains, compared to phthalate dioxygenase reductase and other known systems containing these three domains. In BenC, the ferredoxin domain interacts with both the flavin and NAD(P)H domains. The iron-sulfur center and the flavin are about 9 A apart, which allows a fast electron transfer. The BenC structure is the first determined for a reductase from the class IB Rieske dioxygenases, whose reductases transfer electrons directly to their oxygenase components. Based on sequence similarities, a very similar structure was modeled for the class III naphthalene dioxygenase reductase, which transfers electrons to an intermediary ferredoxin, rather than the oxygenase component. |
==About this Structure== | ==About this Structure== | ||
| - | 1KRH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Acinetobacter_sp. Acinetobacter sp.] with SO4, FES and FAD as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Ferredoxin--NAD(+)_reductase Ferredoxin--NAD(+) reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.18.1.3 1.18.1.3] Full crystallographic information is available from [http:// | + | 1KRH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Acinetobacter_sp. Acinetobacter sp.] with <scene name='pdbligand=SO4:'>SO4</scene>, <scene name='pdbligand=FES:'>FES</scene> and <scene name='pdbligand=FAD:'>FAD</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Ferredoxin--NAD(+)_reductase Ferredoxin--NAD(+) reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.18.1.3 1.18.1.3] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KRH OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Ferredoxin--NAD(+) reductase]] | [[Category: Ferredoxin--NAD(+) reductase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Beharry, Z | + | [[Category: Beharry, Z M.]] |
| - | [[Category: Coulter, E | + | [[Category: Coulter, E D.]] |
| - | [[Category: Eby, D | + | [[Category: Eby, D M.]] |
[[Category: Eklund, H.]] | [[Category: Eklund, H.]] | ||
| - | [[Category: Jr., D | + | [[Category: Jr., D M.Kurtz.]] |
[[Category: Karlsson, A.]] | [[Category: Karlsson, A.]] | ||
| - | [[Category: Niedle, E | + | [[Category: Niedle, E L.]] |
[[Category: Ramaswamy, S.]] | [[Category: Ramaswamy, S.]] | ||
[[Category: FAD]] | [[Category: FAD]] | ||
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[[Category: nadh-binding]] | [[Category: nadh-binding]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:37:11 2008'' |
Revision as of 11:37, 21 February 2008
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X-ray Stucture of Benzoate Dioxygenase Reductase
Overview
One of the major processes for aerobic biodegradation of aromatic compounds is initiated by Rieske dioxygenases. Benzoate dioxygenase contains a reductase component, BenC, that is responsible for the two-electron transfer from NADH via FAD and an iron-sulfur cluster to the terminal oxygenase component. Here, we present the structure of BenC from Acinetobacter sp. strain ADP1 at 1.5 A resolution. BenC contains three domains, each binding a redox cofactor: iron-sulfur, FAD and NADH, respectively. The [2Fe-2S] domain is similar to that of plant ferredoxins, and the FAD and NADH domains are similar to members of the ferredoxin:NADPH reductase superfamily. In phthalate dioxygenase reductase, the only other Rieske dioxygenase reductase for which a crystal structure is available, the ferredoxin-like and flavin binding domains are sequentially reversed compared to BenC. The BenC structure shows significant differences in the location of the ferredoxin domain relative to the other domains, compared to phthalate dioxygenase reductase and other known systems containing these three domains. In BenC, the ferredoxin domain interacts with both the flavin and NAD(P)H domains. The iron-sulfur center and the flavin are about 9 A apart, which allows a fast electron transfer. The BenC structure is the first determined for a reductase from the class IB Rieske dioxygenases, whose reductases transfer electrons directly to their oxygenase components. Based on sequence similarities, a very similar structure was modeled for the class III naphthalene dioxygenase reductase, which transfers electrons to an intermediary ferredoxin, rather than the oxygenase component.
About this Structure
1KRH is a Single protein structure of sequence from Acinetobacter sp. with , and as ligands. Active as Ferredoxin--NAD(+) reductase, with EC number 1.18.1.3 Full crystallographic information is available from OCA.
Reference
X-ray crystal structure of benzoate 1,2-dioxygenase reductase from Acinetobacter sp. strain ADP1., Karlsson A, Beharry ZM, Matthew Eby D, Coulter ED, Neidle EL, Kurtz DM Jr, Eklund H, Ramaswamy S, J Mol Biol. 2002 Apr 26;318(2):261-72. PMID:12051836
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