A flavodoxin that is required for enzyme activation: the structure of oxidized flavodoxin from Escherichia coli at 1.8 A resolution

Protein Science : a Publication of the Protein Society
D M Hoover, M L Ludwig

Abstract

In Escherichia coli, flavodoxin is the physiological electron donor for the reductive activation of the enzymes pyruvate formate-lyase, anaerobic ribonucleotide reductase, and B12-dependent methionine synthase. As a basis for studies of the interactions of flavodoxin with methionine synthase, crystal structures of orthorhombic and trigonal forms of oxidized recombinant flavodoxin from E. coli have been determined. The orthorhombic form (space group P2(1)2(1)2(1), a = 126.4, b = 41.10, c = 69.15 A, with two molecules per asymmetric unit) was solved initially by molecular replacement at a resolution of 3.0 A, using coordinates from the structure of the flavodoxin from Synechococcus PCC 7942 (Anacystis nidulans). Data extending to 1.8-A resolution were collected at 140 K and the structure was refined to an Rwork of 0.196 and an Rfree of 0.250 for reflections with I > 0. The final model contains 3,224 non-hydrogen atoms per asymmetric unit, including 62 flavin mononucleotide (FMN) atoms, 354 water molecules, four calcium ions, four sodium ions, two chloride ions, and two Bis-Tris buffer molecules. The structure of the protein in the trigonal form (space group P312, a = 78.83, c = 52.07 A) was solved by molecular replacement using t...Continue Reading

References

Jan 30, 1977·Archives of Biochemistry and Biophysics·K FujiiF M Huennekens
Sep 1, 1975·Archives of Biochemistry and Biophysics·D C Yoch
Mar 15, 1992·Proceedings of the National Academy of Sciences of the United States of America·E Katchalski-KatzirI A Vakser
Jul 1, 1990·Acta Crystallographica. Section A, Foundations of Crystallography·A T BrüngerJ W Erickson
Apr 20, 1990·Journal of Molecular Biology·Z X Xia, F S Mathews
Nov 1, 1989·The Biochemical Journal·S WakabayashiL J Rogers
Mar 1, 1988·Acta Crystallographica. Section A, Foundations of Crystallography·T O Yeates
Oct 1, 1985·Analytical Biochemistry·P K SmithD C Klenk
Feb 17, 1986·European Journal of Biochemistry·J KlugkistC Veeger
Jan 1, 1985·Methods in Enzymology·R Hamlin
Jan 1, 1985·Methods in Enzymology·A J HowardN H Xuong
Dec 1, 1973·Proceedings of the National Academy of Sciences of the United States of America·K D WatenpaughL H Jensen
Mar 1, 1971·Hoppe-Seyler's Zeitschrift für physiologische Chemie·H Vetter, J Knappe
May 12, 1971·Biochimica Et Biophysica Acta·S G Mayhew
Feb 14, 1971·Journal of Molecular Biology·B Lee, F M Richards
Jun 1, 1968·Archives of Biochemistry and Biophysics·R D Draper, L L Ingraham
Apr 28, 1968·Journal of Molecular Biology·B W Matthews
Feb 1, 1966·Biochemistry·N E GoodR M Singh
Apr 25, 1983·Journal of Molecular Biology·W W SmithK T Yasunobu
May 1, 1980·Proceedings of the National Academy of Sciences of the United States of America·D Nieva-GómezW J Brill
Jul 28, 1995·Science·R D FleischmannJ M Merrick
Aug 15, 1994·European Journal of Biochemistry·O IfukuY Wachi
Dec 28, 1993·Biochemistry·K K WongJ W Kozarich
Dec 15, 1993·Biochemical and Biophysical Research Communications·V BianchiP Reichard

❮ Previous
Next ❯

Citations

Sep 18, 2002·Archives of Biochemistry and Biophysics·Jason T Wan, Joseph T Jarrett
Aug 9, 2001·Proceedings of the National Academy of Sciences of the United States of America·D A HallR G Matthews
Jul 8, 1998·Proceedings of the National Academy of Sciences of the United States of America·M W FischerE R Zuiderweg
Jan 16, 2002·Protein Science : a Publication of the Protein Society·Jörg FreigangRalf Paul
Nov 9, 2014·Journal of Biomolecular NMR·Qian YeChangwen Jin
Nov 26, 2009·Phytochemistry·Kenneth Jensen, Birger Lindberg Møller
Jul 16, 2017·Protein Science : a Publication of the Protein Society·Helen M SegalDouglas C Rees
Sep 29, 2001·The Journal of Biological Chemistry·A K ArakakiE A Ceccarelli
Oct 30, 2004·Chembiochem : a European Journal of Chemical Biology·Frank LöhrHeinz Rüterjans
Mar 14, 2020·International Journal of Molecular Sciences·Sandra Salillas, Javier Sancho
Jun 16, 2001·The Journal of Biological Chemistry·M V Fonseca, J C Escalante-Semerena
May 23, 2019·Protein Science : a Publication of the Protein Society·Robert G MothersoleKirsten R Wolthers
Sep 1, 2005·Protein Science : a Publication of the Protein Society·Sharmini AlagaratnamGerard W Canters
Feb 16, 2005·The Journal of Biological Chemistry·Rajasekhar NeeliAndrew W Munro
Jul 27, 1999·Journal of Bacteriology·M ZhengG Storz
Dec 1, 2004·EcoSal Plus·R Gary Sawers, David P Clark
Jul 9, 2002·Biochimica Et Biophysica Acta·Christian K EngelGilbert G Privé
Sep 1, 2008·EcoSal Plus·Jorge C Escalante-Semerena, Martin J Warren
Nov 24, 2004·Biochemical and Biophysical Research Communications·Sinead C HanleySimon Daff
Oct 2, 2007·Archives of Biochemistry and Biophysics·Susana FragoMilagros Medina
Aug 12, 2009·Biochimica Et Biophysica Acta·Julie WolfovaJannette Carey
May 12, 2010·Journal of Structural Biology·Sara Ayuso-TejedorJavier Sancho

❮ Previous
Next ❯

Related Concepts

Trending Feeds

COVID-19

Coronaviruses encompass a large family of viruses that cause the common cold as well as more serious diseases, such as the ongoing outbreak of coronavirus disease 2019 (COVID-19; formally known as 2019-nCoV). Coronaviruses can spread from animals to humans; symptoms include fever, cough, shortness of breath, and breathing difficulties; in more severe cases, infection can lead to death. This feed covers recent research on COVID-19.

Blastomycosis

Blastomycosis fungal infections spread through inhaling Blastomyces dermatitidis spores. Discover the latest research on blastomycosis fungal infections here.

Nuclear Pore Complex in ALS/FTD

Alterations in nucleocytoplasmic transport, controlled by the nuclear pore complex, may be involved in the pathomechanism underlying multiple neurodegenerative diseases including Amyotrophic Lateral Sclerosis and Frontotemporal Dementia. Here is the latest research on the nuclear pore complex in ALS and FTD.

Applications of Molecular Barcoding

The concept of molecular barcoding is that each original DNA or RNA molecule is attached to a unique sequence barcode. Sequence reads having different barcodes represent different original molecules, while sequence reads having the same barcode are results of PCR duplication from one original molecule. Discover the latest research on molecular barcoding here.

Chronic Fatigue Syndrome

Chronic fatigue syndrome is a disease characterized by unexplained disabling fatigue; the pathology of which is incompletely understood. Discover the latest research on chronic fatigue syndrome here.

Evolution of Pluripotency

Pluripotency refers to the ability of a cell to develop into three primary germ cell layers of the embryo. This feed focuses on the mechanisms that underlie the evolution of pluripotency. Here is the latest research.

Position Effect Variegation

Position Effect Variagation occurs when a gene is inactivated due to its positioning near heterochromatic regions within a chromosome. Discover the latest research on Position Effect Variagation here.

STING Receptor Agonists

Stimulator of IFN genes (STING) are a group of transmembrane proteins that are involved in the induction of type I interferon that is important in the innate immune response. The stimulation of STING has been an active area of research in the treatment of cancer and infectious diseases. Here is the latest research on STING receptor agonists.

Microbicide

Microbicides are products that can be applied to vaginal or rectal mucosal surfaces with the goal of preventing, or at least significantly reducing, the transmission of sexually transmitted infections. Here is the latest research on microbicides.