1krh
From Proteopedia
OCA (Talk | contribs)
(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...)
Next diff →
Revision as of 17:37, 20 November 2007
|
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 SO4, FES and FAD 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
Page seeded by OCA on Tue Nov 20 19:44:49 2007
