1FQT

CRYSTAL STRUCTURE OF THE RIESKE-TYPE FERREDOXIN ASSOCIATED WITH BIPHENYL DIOXYGENASE

Summary for 1FQT

• Entry DOI: 10.2210/pdb1fqt/pdb
• Related: 1NDO 1RFS 1RIE
• Descriptor: RIESKE-TYPE FERREDOXIN OF BIPHENYL DIOXYGENASE, FE2/S2 (INORGANIC) CLUSTER, GLYCEROL, ... (4 entities in total)
• Functional Keywords: rieske-type ferredoxin, 2fe-2s cluster, beta sandwich, oxidoreductase
• Biological source: Burkholderia xenovorans
• Total number of polymer chains: 2
• Total formula weight: 25129.55

Authors

Colbert, C.L.,Couture, M.M.-J.,Eltis, L.D.,Bolin, J.T. (deposition date: 2000-09-06, release date: 2001-01-03, Last modification date: 2024-02-07)

Primary citation

Colbert, C.L.,Couture, M.M.,Eltis, L.D.,Bolin, J.T.
A cluster exposed: structure of the Rieske ferredoxin from biphenyl dioxygenase and the redox properties of Rieske Fe-S proteins.
Structure Fold.Des., 8:1267-1278, 2000

PubMed Abstract: Ring-hydroxylating dioxygenases are multicomponent systems that initiate biodegradation of aromatic compounds. Many dioxygenase systems include Rieske-type ferredoxins with amino acid sequences and redox properties remarkably different from the Rieske proteins of proton-translocating respiratory and photosynthetic complexes. In the latter, the [Fe2S2] clusters lie near the protein surface, operate at potentials above +300 mV at pH 7, and express pH- and ionic strength-dependent redox behavior. The reduction potentials of the dioxygenase ferredoxins are approximately 150 mV and are pH-independent. These distinctions were predicted to arise from differences in the exposure of the cluster and/or interactions of the histidine ligands.

PubMed: 11188691
DOI: 10.1016/S0969-2126(00)00536-0

Experimental method

X-RAY DIFFRACTION (1.6 Å)