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1.18.1.5: putidaredoxin-NAD+ reductase

This is an abbreviated version!
For detailed information about putidaredoxin-NAD+ reductase, go to the full flat file.

Word Map on EC 1.18.1.5

Reaction

reduced putidaredoxin
+
NAD+
=
oxidized putidaredoxin
 +
NADH
 +
H+

Synonyms

camA, Pdr, putidaredoxin reductase

ECTree

     1 Oxidoreductases
         1.18 Acting on iron-sulfur proteins as donors
             1.18.1 With NAD+ or NADP+ as acceptor
                1.18.1.5 putidaredoxin-NAD+ reductase

Crystallization

Crystallization on EC 1.18.1.5 - putidaredoxin-NAD+ reductase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
computational modeling based on crystal structures of putidaredoxin Ptxand putidaredoxin reductase PdR. In the model, Pdx is docked above the isoalloxazine ring of FAD of Pdr with the distance between the flavin and [2Fe-2S] of 14.6 A. This mode of interaction allows Pdx to easily adjust and optimize orientation of its cofactor relative to Pdr. The key residues of Pdx located at the center are Asp38 and Trp106, and at the edge of the protein-protein interface are Tyr33 and Arg66
crystal structure of a covalently linked putidaredoxin reductase (Pdr)-putidaredoxin (Pdx) complex. Residues R65 and R310 are the key elements required for the formation of a productive electron transfer complex with Pdx. The C-terminal lysine cluster assists in Pdx docking by fine-tuning Pdr-Pdx interactions to achieve the optimal geometry between the redox centers, and the basic surface residues in Pdr-like ferredoxin reductases not only define specificity for the redox partner but also may facilitate its dissociation
crystal structures of C73S/C85S and C73S mutants, to 1.47 A and 1.65 A resolution, respectively, are nearly identical and very similar to those of bovine adrenodoxin and Escherichia coli ferredoxin. In particular, formation of a hydrogen bond between the side-chain of Y51 and the carbonyl oxygen atom of E77 and the presence of two well-ordered water molecules linking the interaction domain and the C-terminal peptide to the core of the molecule are unique to Pdx. The folding topology of the NMR model is similar to that of the X-ray structure of Pdx. W106, important in the Pdr-to-Pdx and Pdx-to-P450cam electron transfer reactions, is in a position to regulate and/or mediate electron transfer to or from the [2Fe–2S] center of Pdx
mutant C73G, to 1.9 A resolution. The C2 crystal contains three putidaredoxin molecules in the asymmetric unit. Findings show a unanimous structure in some regions crucial for electron-transfer interactions, including the cluster-binding loop 39-48 and the cytochrome-interaction region of Asp38 and Trp106. In addition, the Cys45 amide group donates a hydrogen bond to cluster sulfur S1, with Ala46 adopting an Lalpha conformation
-
sitting drop vapour diffusion method with 1.5 M lithium sulfate, 0.15 M lithium acetate, 0.1 M lithium formate, 2% (v/v) glycerol, 1 mM dithiothreitol, and 0.1 M Bis-Tris-propane (pH 8.0)