3MHP

FNR-recruitment to the thylakoid

Summary for 3MHP

• Entry DOI: 10.2210/pdb3mhp/pdb
• Related: 1QFY 1QFZ 1QG0 1QGA
• Descriptor: Ferredoxin--NADP reductase, leaf isozyme, chloroplastic, TIC62_peptide, FLAVIN-ADENINE DINUCLEOTIDE, ... (4 entities in total)
• Functional Keywords: fnr, oxidoreductase, thylakoid membrane, proton-flux, poly proline ii helix, self assembly, nadp(h)
• Biological source: Pisum sativum (garden pea,peas); More
• Cellular location: Plastid, chloroplast stroma: P10933
• Total number of polymer chains: 3
• Total formula weight: 71548.46

Authors

Groll, M.,Alte, F.,Soll, J.,Boelter, B. (deposition date: 2010-04-08, release date: 2010-10-27, Last modification date: 2023-09-06)

Primary citation

Alte, F.,Stengel, A.,Benz, J.P.,Petersen, E.,Soll, J.,Groll, M.,Bolter, B.
Ferredoxin:NADPH oxidoreductase is recruited to thylakoids by binding to a polyproline type II helix in a pH-dependent manner.
Proc.Natl.Acad.Sci.USA, 107:19260-19265, 2010

PubMed Abstract: Ferredoxin:NADPH oxidoreductase (FNR) is a key enzyme of photosynthetic electron transport required for generation of reduction equivalents. Recently, two proteins were found to be involved in membrane-anchoring of FNR by specific interaction via a conserved Ser/Pro-rich motif: Tic62 and Trol. Our crystallographic study reveals that the FNR-binding motif, which forms a polyproline type II helix, induces self-assembly of two FNR monomers into a back-to-back dimer. Because binding occurs opposite to the FNR active sites, its activity is not affected by the interaction. Surface plasmon resonance analyses disclose a high affinity of FNR to the binding motif, which is strongly increased under acidic conditions. The pH of the chloroplast stroma changes dependent on the light conditions from neutral to slightly acidic in complete darkness or to alkaline at saturating light conditions. Recruiting of FNR to the thylakoids could therefore represent a regulatory mechanism to adapt FNR availability/activity to photosynthetic electron flow.

PubMed: 20974920
DOI: 10.1073/pnas.1009124107

Experimental method

X-RAY DIFFRACTION (1.7 Å)