3w5v

Cross-linked complex between Ferredoxin and Ferredoxin-NADP+ reductase

spinqualitylabelsall models 3w5v, resolution 3.81Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3w5v is a 4 chain structure with sequence from Zea mays. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 3.81Å Ligands: FAD, FES Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function FER1_MAIZE Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions. Publication Abstract from PubMed Ferredoxin-NADP(+) reductase (FNR) forms a 1:1 complex with ferredoxin (Fd), and catalyzes the electron transfer between Fd and NADP(+). In our previous study, we prepared a series of site-specifically cross-linked complexes of Fd and FNR, which showed diverse electron transfer properties. Here, we show that X-ray crystal structures of the two different Fd-FNR cross-linked complexes form oligomers by swapping Fd and FNR moieties across the molecules; one complex is a dimer from, and the other is a successive multimeric form. In order to verify whether these oligomeric structures are formed only in crystal, we investigated the possibility of the oligomerization of these complexes in solution. The mean values of the particle size of these cross-linked complexes were shown to increase with the rise of protein concentration at sub-milimolar order, whereas the size of dissociable wild-type Fd:FNR complex was unchanged as analyzed by dynamic light scattering measurement. The oligomerization products were detected by SDS-PAGE after chemical cross-linking of these complexes at the sub-milimolar concentrations. The extent and concentration-dependent profile of the oligomerizaion were differentiated between the two cross-linked complexes. These results show that these Fd-FNR cross-linked complexes exhibit concentration-dependent oligomerization, possibly through swapping of Fd and FNR moieties also in solution. These findings lead to the possibility that some native multi-domain proteins may present similar phenomenon in vivo. Concentration-dependent oligomerization of cross-linked complexes between ferredoxin and ferredoxin-NADP(+) reductase.,Kimata-Ariga Y, Kubota-Kawai H, Lee YH, Muraki N, Ikegami T, Kurisu G, Hase T Biochem Biophys Res Commun. 2013 May 17;434(4):867-72. doi:, 10.1016/j.bbrc.2013.04.033. Epub 2013 Apr 22. PMID:23618857 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Ferredoxin 3D structures

Proteopedia Page Contributors and Editors (what is this?)

OCA