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3LB8

Crystal structure of the covalent putidaredoxin reductase-putidaredoxin complex

Summary for 3LB8
Entry DOI10.2210/pdb3lb8/pdb
Related1OQQ 1Q1R
DescriptorPutidaredoxin reductase, Putidaredoxin, FLAVIN-ADENINE DINUCLEOTIDE, ... (5 entities in total)
Functional Keywordscovalently linked protein-protein complex, fad, flavoprotein, oxidoreductase, electron transport, iron-sulfur, metal-binding, oxidoreductase-electron transport complex, oxidoreductase/electron transport
Biological sourcePseudomonas putida
More
Total number of polymer chains4
Total formula weight119247.69
Authors
Sevrioukova, I.F. (deposition date: 2010-01-07, release date: 2010-02-23, Last modification date: 2024-11-06)
Primary citationSevrioukova, 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: 20179327
DOI: 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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数据于2025-07-23公开中

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