2RC6

Refined structure of FNR from Leptospira interrogans bound to NADP+

Summary for 2RC6

• Entry DOI: 10.2210/pdb2rc6/pdb
• Related: 2RC5
• Descriptor: Ferredoxin-NADP reductase, ZINC ION, SULFATE ION, ... (6 entities in total)
• Functional Keywords: fnr, oxidoreductase
• Biological source: Leptospira interrogans
• Total number of polymer chains: 4
• Total formula weight: 146818.13

Authors

Nascimento, A.S.,Catalano-Dupuy, D.L.,Ceccarelli, E.A.,Polikarpov, I. (deposition date: 2007-09-19, release date: 2008-03-25, Last modification date: 2024-02-21)

Primary citation

Nascimento, A.S.,Catalano-Dupuy, D.L.,Bernardes, A.,Neto, M.O.,Santos, M.A.,Ceccarelli, E.A.,Polikarpov, I.
Crystal structures of Leptospira interrogans FAD-containing ferredoxin-NADP+ reductase and its complex with NADP+.
Bmc Struct.Biol., 7:69-69, 2007

PubMed Abstract: Ferredoxin-NADP(H) reductases (FNRs) are flavoenzymes that catalyze the electron transfer between NADP(H) and the proteins ferredoxin or flavodoxin. A number of structural features distinguish plant and bacterial FNRs, one of which is the mode of the cofactor FAD binding. Leptospira interrogans is a spirochaete parasitic bacterium capable of infecting humans and mammals in general. Leptospira interrogans FNR (LepFNR) displays low sequence identity with plant (34% with Zea mays) and bacterial (31% with Escherichia coli) FNRs. However, LepFNR contains all consensus sequences that define the plastidic class FNRs.

PubMed: 17958910
DOI: 10.1186/1472-6807-7-69

Experimental method

X-RAY DIFFRACTION (2.7 Å)