3B2F

Maize Ferredoxin 1

Summary for 3B2F

• Entry DOI: 10.2210/pdb3b2f/pdb
• Related: 1GAQ 3B2G
• Descriptor: Ferredoxin-1, chloroplastic, FE2/S2 (INORGANIC) CLUSTER (3 entities in total)
• Functional Keywords: electron transfer, fnr, nir, sir, fd-gogat, electron transport
• Biological source: Zea mays (maize)
• Cellular location: Plastid, chloroplast: P27787
• Total number of polymer chains: 2
• Total formula weight: 21388.38

Authors

Kurisu, G.,Hase, T. (deposition date: 2011-08-01, release date: 2012-06-13, Last modification date: 2024-03-13)

Primary citation

Sakakibara, Y.,Kimura, H.,Iwamura, A.,Saitoh, T.,Ikegami, T.,Kurisu, G.,Hase, T.
A new structural insight into differential interaction of cyanobacterial and plant ferredoxins with nitrite reductase as revealed by NMR and X-ray crystallographic studies
J.Biochem., 151:483-492, 2012

PubMed Abstract: Ferredoxin (Fd), which plays a pivotal role in photosynthesis as an electron carrier, forms a transient complex with various Fd-dependent enzymes, such as nitrite reductase (NiR), to achieve efficient intermolecular electron transfer. We studied the protein-protein interaction of Fd and NiR by NMR spectroscopy and determined three acidic regions of Fd to be major sites for the interaction with NiR, indicating that the complex is stabilized through electrostatic interaction. During this study, we found Fds from higher plant and cyanobacterium, in spite of their high structural similarities including the above acidic regions, differ remarkably in the interaction with cyanobacterial NiR. In activity assay of NiR, K(m) value for maize Fd (74.6 µM) was 9.6 times larger than that for Leptolyngbya boryana Fd (7.8 µM). The two Fds also showed a similar difference in binding assay to NiR-immobilized resin. Comparative site-specific mutagenesis of two Fds revealed that their discriminative ability for the interaction with NiR is attributed mainly to non-charged residues in the peripheral region of [2Fe-2S] cluster. These non-charged residues are conserved separately between Fds of plant and cyanobacterial origins. Our data highlight that intermolecular force(s) other than electrostatic attraction is(are) also crucial for the molecular interaction between Fd and partner enzyme.

PubMed: 22427434
DOI: 10.1093/jb/mvs028

Experimental method

X-RAY DIFFRACTION (1.7 Å)