3LB8
Crystal structure of the covalent putidaredoxin reductase-putidaredoxin complex
Summary for 3LB8
Entry DOI | 10.2210/pdb3lb8/pdb |
Related | 1OQQ 1Q1R |
Descriptor | Putidaredoxin reductase, Putidaredoxin, FLAVIN-ADENINE DINUCLEOTIDE, ... (5 entities in total) |
Functional Keywords | covalently linked protein-protein complex, fad, flavoprotein, oxidoreductase, electron transport, iron-sulfur, metal-binding, oxidoreductase-electron transport complex, oxidoreductase/electron transport |
Biological source | Pseudomonas putida More |
Total number of polymer chains | 4 |
Total formula weight | 119247.69 |
Authors | Sevrioukova, I.F. (deposition date: 2010-01-07, release date: 2010-02-23, Last modification date: 2024-11-06) |
Primary citation | Sevrioukova, I.F.,Poulos, T.L.,Churbanova, I.Y. Crystal structure of the putidaredoxin reductase x putidaredoxin electron transfer complex. J.Biol.Chem., 285:13616-13620, 2010 Cited by PubMed Abstract: In the camphor monooxygenase system from Pseudomonas putida, the [2Fe-2S]-containing putidaredoxin (Pdx) shuttles electrons between the NADH-dependent putidaredoxin reductase (Pdr) and cytochrome P450(cam). The mechanism of the Pdr.Pdx redox couple has been investigated by a variety of techniques. One of the exceptions is x-ray crystallography as the native partners associate weakly and resist co-crystallization. Here, we present the 2.6-A x-ray structure of a catalytically active complex between Pdr and Pdx C73S/C85S chemically cross-linked via the Lys(409Pdr)-Glu(72Pdx) pair. The 365 A(2) Pdr-Pdx interface is predominantly hydrophobic with one central Arg(310Pdr)-Asp(38Pdx) salt bridge, likely assisting docking and orienting the partners optimally for electron transfer, and a few peripheral hydrogen bonds. A predicted 12-A-long electron transfer route between FAD and [2Fe-2S] includes flavin flanking Trp(330Pdr) and the iron ligand Cys(39Pdx). The x-ray model agrees well with the experimental and theoretical results and suggests that the linked Pdx must undergo complex movements during turnover to accommodate P450(cam), which could limit the Pdx-to-P450(cam) electron transfer reaction. PubMed: 20179327DOI: 10.1074/jbc.M110.104968 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.6 Å) |
Structure validation
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