1GR1

Structure of Ferredoxin-NADP+ Reductase with Glu 139 replaced by Lys (E139K)

Summary for 1GR1

• Entry DOI: 10.2210/pdb1gr1/pdb
• Related: 1B2R 1BJK 1BQE 1E62 1E63 1E64 1EWY 1GJR 1GO2 1H42 1H85 1QGZ 1QH0 1QUE 1QUF
• Descriptor: FERREDOXIN--NADP+ REDUCTASE, FLAVIN-ADENINE DINUCLEOTIDE, SULFATE ION, ... (4 entities in total)
• Functional Keywords: oxidoreductase, flavoprotein, fad, fnr, nadp+ reductase
• Biological source: NOSTOC SP. PCC7119
• Total number of polymer chains: 1
• Total formula weight: 34923.36

Authors

Hermoso, J.A.,Mayoral, T.,Medina, M.,Sanz-Aparicio, J.,Gomez-Moreno, C. (deposition date: 2001-12-12, release date: 2002-10-24, Last modification date: 2023-12-13)

Primary citation

Faro, M.,Frago, S.,Mayoral, T.,Hermoso, J.A.,Sanz-Aparico, J.,Gomez-Moreno, C.,Medina, M.
Probing the Role of Glutamic Acid 139 of Anabena Ferrodoxin-Nadp+ Reductase in the Interaction with Substrates
Eur.J.Biochem., 269:4938-, 2002

PubMed Abstract: The role of the negative charge of the E139 side-chain of Anabaena Ferredoxin-NADP+ reductase (FNR) in steering appropriate docking with its substrates ferredoxin, flavodoxin and NADP+/H, that leads to efficient electron transfer (ET) is analysed by characterization of several E139 FNR mutants. Replacement of E139 affects the interaction with the different FNR substrates in very different ways. Thus, while E139 does not appear to be involved in the processes of binding and ET between FNR and NADP+/H, the nature and the conformation of the residue at position 139 of Anabaena FNR modulates the precise enzyme interaction with the protein carriers ferredoxin (Fd) and flavodoxin (Fld). Introduction of the shorter aspartic acid side-chain at position 139 produces an enzyme that interacts more weakly with both ET proteins. Moreover, the removal of the charge, as in the E139Q mutant, or the charge-reversal mutation, as in E139K FNR, apparently enhances additional interaction modes of the enzyme with Fd, and reduces the possible orientations with Fld to more productive and stronger ones. Hence, removal of the negative charge at position 139 of Anabaena FNR produces a deleterious effect in its ET reactions with Fd whereas it appears to enhance the ET processes with Fld. Significantly, a large structural variation is observed for the E139 side-chain conformer in different FNR structures, including the E139K mutant. In this case, a positive potential region replaces a negative one in the wild-type enzyme. Our observations further confirm the contribution of both attractive and repulsive interactions in achieving the optimal orientation for efficient ET between FNR and its protein carriers.

PubMed: 12383252
DOI: 10.1046/J.1432-1033.2002.03194.X

Experimental method

X-RAY DIFFRACTION (2.5 Å)