2rc5
From Proteopedia
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'''Refined structure of FNR from Leptospira interrogans''' | '''Refined structure of FNR from Leptospira interrogans''' | ||
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==Reference== | ==Reference== | ||
Crystal structures of Leptospira interrogans FAD-containing ferredoxin-NADP+ reductase and its complex with NADP+., Nascimento AS, Catalano-Dupuy DL, Bernardes A, Neto Mde O, Santos MA, Ceccarelli EA, Polikarpov I, BMC Struct Biol. 2007 Oct 24;7:69. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17958910 17958910] | Crystal structures of Leptospira interrogans FAD-containing ferredoxin-NADP+ reductase and its complex with NADP+., Nascimento AS, Catalano-Dupuy DL, Bernardes A, Neto Mde O, Santos MA, Ceccarelli EA, Polikarpov I, BMC Struct Biol. 2007 Oct 24;7:69. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17958910 17958910] | ||
| - | [[Category: Ferredoxin--NADP(+) reductase]] | ||
[[Category: Leptospira interrogans]] | [[Category: Leptospira interrogans]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: Nascimento, A S.]] | [[Category: Nascimento, A S.]] | ||
[[Category: Polikarpov, I.]] | [[Category: Polikarpov, I.]] | ||
| - | [[Category: | + | [[Category: Fad]] |
| - | [[Category: | + | [[Category: Oxidoreductase]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 16:37:51 2008'' | |
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Revision as of 13:37, 4 May 2008
Refined structure of FNR from Leptospira interrogans
Overview
BACKGROUND: 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. RESULTS: The crystal structures of the FAD-containing LepFNR and the complex of the enzyme with NADP+, were solved and compared to known FNRs. The comparison reveals significant structural similarities of the enzyme with the plastidic type FNRs and differences with the bacterial enzymes. Our small angle X-ray scattering experiments show that LepFNR is a monomeric enzyme. Moreover, our biochemical data demonstrate that the LepFNR has an enzymatic activity similar to those reported for the plastidic enzymes and that is significantly different from bacterial flavoenzymes, which display lower turnover rates. CONCLUSION: LepFNR is the first plastidic type FNR found in bacteria and, despite of its low sequence similarity with plastidic FNRs still displays high catalytic turnover rates. The typical structural and biochemical characteristics of plant FNRs unveiled for LepFNR support a notion of a putative lateral gene transfer which presumably offers Leptospira interrogans evolutionary advantages. The wealth of structural information about LepFNR provides a molecular basis for advanced drugs developments against leptospirosis.
About this Structure
2RC5 is a Single protein structure of sequence from Leptospira interrogans. Full crystallographic information is available from OCA.
Reference
Crystal structures of Leptospira interrogans FAD-containing ferredoxin-NADP+ reductase and its complex with NADP+., Nascimento AS, Catalano-Dupuy DL, Bernardes A, Neto Mde O, Santos MA, Ceccarelli EA, Polikarpov I, BMC Struct Biol. 2007 Oct 24;7:69. PMID:17958910 Page seeded by OCA on Sun May 4 16:37:51 2008
