Related ArticlesNMR assignments, secondary structure and hydration of oxidized Escherichia coli flavodoxin.
Eur J Biochem. 1997 Mar 1;244(2):384-99
Authors: Ponstingl H, Otting G
Recombinant flavodoxin from Escherichia coli was uniformly enriched with 15N and 13C isotopes and its oxidized form in aqueous solution investigated by three-dimensional NMR spectroscopy. Nearly complete 1H, 15N and 13C resonance assignments were obtained. The secondary structure was determined from chemical shift, NOE and 3J(HNH alpha) coupling constant data. Like homologous long-chain flavodoxins, E. coli flavodoxin contains a five-stranded parallel beta-sheet and five helices. The beta-strands were found to comprise the residues 3-8, 29-34, 48-56, 80-89, 114-116 and 141-145. The helices comprise residues 12-25, 40-45, 62-73, 98-108 and 152-166. The FMN-binding site was determined by intermolecular NOEs and low-field shifted amide proton resonances induced by the phosphoester group of the cofactor. The data are in good agreement with a previously predicted model of E. coli flavodoxin [Havel, T. F. (1993) Mol. Sim. 10, 175-210]. The analysis of of water-flavodoxin NOEs revealed the presence of two, possibly three, buried hydration water molecules which are located at sites, where homologous flavodoxins from Anacystis nidulans and Anabena 7120 contain conserved hydration water molecules. One of these water molecules mediates hydrogen bonds between the protein backbone and the ribityl chain of the FMN cofactor.
[NMR paper] Multinuclear NMR resonance assignments and the secondary structure of Escherichia col
Multinuclear NMR resonance assignments and the secondary structure of Escherichia coli thioesterase/protease I: a member of a new subclass of lipolytic enzymes.
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J Biomol NMR. 1998 May;11(4):363-80
Authors: Lin TH, Chen C, Huang RF, Lee YL, Shaw JF, Huang TH
Escherichia coli thioesterase/protease I is a 183 amino acid protein with a molecular mass of 20,500. This...
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[NMR paper] NMR assignments, secondary structure and hydration of oxidized Escherichia coli flavo
NMR assignments, secondary structure and hydration of oxidized Escherichia coli flavodoxin.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif Related Articles NMR assignments, secondary structure and hydration of oxidized Escherichia coli flavodoxin.
Eur J Biochem. 1997 Mar 1;244(2):384-99
Authors: Ponstingl H, Otting G
Recombinant flavodoxin from Escherichia coli was uniformly enriched with 15N and 13C isotopes and its oxidized form in aqueous...
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[NMR paper] 1H and 15N NMR resonance assignments and solution secondary structure of oxidized Des
1H and 15N NMR resonance assignments and solution secondary structure of oxidized Desulfovibrio desulfuricans flavodoxin.
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J Biomol NMR. 1996 May;7(3):225-35
Authors: Pollock JR, Swenson RP, Stockman BJ
Sequence-specific 1H and 15N resonance assignments have been made for 137 of the 146 nonprolyl residues in oxidized Desulfovibrio desulfuricans flavodoxin. Assignments were obtained by a concerted analysis...
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[NMR paper] Sequential assignments and identification of secondary structure elements of the coli
Sequential assignments and identification of secondary structure elements of the colicin E9 immunity protein in solution by homonuclear and heteronuclear NMR.
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Biochemistry. 1994 Oct 18;33(41):12347-55
Authors: Osborne MJ, Lian LY, Wallis R, Reilly A, James R, Kleanthous C, Moore GR
1H-1H, 1H-15N, and 1H-1H-15N multidimensional NMR spectroscopic studies of the 86 amino...
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[NMR paper] Backbone assignments and secondary structure of the Escherichia coli enzyme-II mannit
Backbone assignments and secondary structure of the Escherichia coli enzyme-II mannitol A domain determined by heteronuclear three-dimensional NMR spectroscopy.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Backbone assignments and secondary structure of the Escherichia coli enzyme-II mannitol A domain determined by heteronuclear three-dimensional...
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[NMR paper] 1H and 15N resonance assignments and solution secondary structure of oxidized Desulfo
1H and 15N resonance assignments and solution secondary structure of oxidized Desulfovibrio vulgaris flavodoxin determined by heteronuclear three-dimensional NMR spectroscopy.
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J Biomol NMR. 1993 Mar;3(2):133-49
Authors: Stockman BJ, Euvrard A, Kloosterman DA, Scahill TA, Swenson RP
Sequence-specific 1H and 15N resonance assignments have been made for all...
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[NMR paper] NMR structure of oxidized Escherichia coli glutaredoxin: comparison with reduced E. c
NMR structure of oxidized Escherichia coli glutaredoxin: comparison with reduced E. coli glutaredoxin and functionally related proteins.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles NMR structure of oxidized Escherichia coli glutaredoxin: comparison with reduced E. coli glutaredoxin and functionally related proteins.
Protein Sci. 1992...
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[NMR paper] Assignment of the 15N NMR spectra of reduced and oxidized Escherichia coli thioredoxi
Assignment of the 15N NMR spectra of reduced and oxidized Escherichia coli thioredoxin.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Assignment of the 15N NMR spectra of reduced and oxidized Escherichia coli thioredoxin.
FEBS Lett. 1991 Jun 24;284(2):178-83
Authors: Chandrasekhar K, Krause G, Holmgren A, Dyson HJ
As a necessary first step in the use of heteronuclear correlated spectra to obtain high resolution solution structures of the protein, assignment of the...