Related ArticlesStructural changes caused by site-directed mutagenesis of tyrosine-98 in Desulfovibrio vulgaris flavodoxin delineated by 1H and 15N NMR spectroscopy: implications for redox potential modulation.
Biochemistry. 1994 Dec 27;33(51):15298-308
Authors: Stockman BJ, Richardson TE, Swenson RP
Flavodoxins mediate electron transfer at low redox potential between the prosthetic groups of other proteins. Interactions between the protein and the flavin mononucleotide cofactor shift both the oxidized/semiquinone and semiquinone/hydroquinone redox potentials significantly from their free-in-solution values. In order to investigate the possible role that the tyrosine at position 98 plays in this process, we have used heteronuclear three-dimensional NMR spectroscopy to determine the solution conformation of wild-type and four position-98 mutants, Y98W, Y98H, Y98A, and Y98R, of Desulfovibrio vulgaris flavodoxin. Assigned 1H and 15N resonances indicate that the secondary structure and topology of the proteins are identical. However, residues that undergo substantial mutation-induced changes in chemical shift are spread throughout the flavin cofactor binding site. Distance and dihedral angle constraints were used to generate solution structures for the wild-type and mutant proteins. Collectively, the mutant proteins have no gross conformational changes in the flavin binding site. The changes that do occur are minor and result from the different packing interactions required to accommodate the new side chain at position-98. The solvent accessibility and electrostatic nature of the flavin binding site in the mutant proteins are compared to those of the wild-type structure. The structural data support the hypothesis that the very low midpoint of the semiquinone/hydroquinone couple in the wild-type protein is modulated to a large extent by the energetically unfavorable formation of the flavin hydroquinone anion in the apolar environment of the flavin binding site.
[NMR paper] Kinetic, Raman, NMR, and site-directed mutagenesis studies of the Pseudomonas sp. str
Kinetic, Raman, NMR, and site-directed mutagenesis studies of the Pseudomonas sp. strain CBS3 4-hydroxybenzoyl-CoA thioesterase active site.
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Biochemistry. 2002 Sep 17;41(37):11152-60
Authors: Zhuang Z, Song F, Zhang W, Taylor K, Archambault A, Dunaway-Mariano D, Dong J, Carey PR
4-Hydroxybenzoyl-coenzyme A (4-HBA-CoA) thioesterase catalyzes the hydrolysis of 4-HBA-CoA to 4-hydroxybenzoate...
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[NMR paper] Structural consequences of site-directed mutagenesis in flexible protein domains: NMR
Structural consequences of site-directed mutagenesis in flexible protein domains: NMR characterization of the L(55,56)S mutant of RhoGDI.
Related Articles Structural consequences of site-directed mutagenesis in flexible protein domains: NMR characterization of the L(55,56)S mutant of RhoGDI.
Eur J Biochem. 2001 Apr;268(8):2253-60
Authors: Golovanov AP, Hawkins D, Barsukov I, Badii R, Bokoch GM, Lian LY, Roberts GC
The guanine dissociation inhibitor RhoGDI consists of a folded C-terminal domain and a highly flexible N-terminal region, both of...
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[NMR paper] The binding site for UCH-L3 on ubiquitin: mutagenesis and NMR studies on the complex
The binding site for UCH-L3 on ubiquitin: mutagenesis and NMR studies on the complex between ubiquitin and UCH-L3.
Related Articles The binding site for UCH-L3 on ubiquitin: mutagenesis and NMR studies on the complex between ubiquitin and UCH-L3.
J Mol Biol. 1999 Sep 3;291(5):1067-77
Authors: Wilkinson KD, Laleli-Sahin E, Urbauer J, Larsen CN, Shih GH, Haas AL, Walsh ST, Wand AJ
The ubiquitin fold is a versatile and widely used targeting signal that is added post-translationally to a variety of proteins. Covalent attachment of one or more...
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[NMR paper] Molecular analysis of sialoside binding to sialoadhesin by NMR and site-directed muta
Molecular analysis of sialoside binding to sialoadhesin by NMR and site-directed mutagenesis.
Related Articles Molecular analysis of sialoside binding to sialoadhesin by NMR and site-directed mutagenesis.
Biochem J. 1999 Jul 15;341 ( Pt 2):355-61
Authors: Crocker PR, Vinson M, Kelm S, Drickamer K
The molecular interactions between sialoadhesin and sialylated ligands have been investigated by using proton NMR. Addition of ligands to the 12 kDa N-terminal immunoglobulin-like domain of sialoadhesin result in resonance shifts in the protein...
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[NMR paper] Heparin binding to platelet factor-4. An NMR and site-directed mutagenesis study: arg
Heparin binding to platelet factor-4. An NMR and site-directed mutagenesis study: arginine residues are crucial for binding.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Heparin binding to platelet factor-4. An NMR and site-directed mutagenesis study: arginine residues are crucial for binding.
Biochem J. 1995 Dec 1;312 ( Pt 2):357-65
Authors: Mayo KH, Ilyina E, Roongta V, Dundas M, Joseph J, Lai CK, Maione T, Daly TJ
Native platelet factor-4 (PF4) is an...
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[NMR paper] Site-directed mutagenesis, fluorescence, and two-dimensional NMR studies on microenvi
Site-directed mutagenesis, fluorescence, and two-dimensional NMR studies on microenvironments of effector region aromatic residues of human c-Ha-Ras protein.
Related Articles Site-directed mutagenesis, fluorescence, and two-dimensional NMR studies on microenvironments of effector region aromatic residues of human c-Ha-Ras protein.
Biochemistry. 1994 Jan 11;33(1):65-73
Authors: Yamasaki K, Shirouzu M, Muto Y, Fujita-Yoshigaki J, Koide H, Ito Y, Kawai G, Hattori S, Yokoyama S, Nishimura S
The Tyr residues in positions 32 and 40 of human c-Ha-Ras...
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[NMR paper] Site-directed mutagenesis, fluorescence, and two-dimensional NMR studies on microenvi
Site-directed mutagenesis, fluorescence, and two-dimensional NMR studies on microenvironments of effector region aromatic residues of human c-Ha-Ras protein.
Related Articles Site-directed mutagenesis, fluorescence, and two-dimensional NMR studies on microenvironments of effector region aromatic residues of human c-Ha-Ras protein.
Biochemistry. 1994 Jan 11;33(1):65-73
Authors: Yamasaki K, Shirouzu M, Muto Y, Fujita-Yoshigaki J, Koide H, Ito Y, Kawai G, Hattori S, Yokoyama S, Nishimura S
The Tyr residues in positions 32 and 40 of human c-Ha-Ras...
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[NMR paper] A proton-NMR study of a site-directed mutation (His388----Glu) in the interdomain reg
A proton-NMR study of a site-directed mutation (His388----Glu) in the interdomain region of yeast phosphoglycerate kinase. Implications for domain movement.
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 A proton-NMR study of a site-directed mutation (His388----Glu) in the interdomain region of yeast phosphoglycerate kinase. Implications for domain movement.
Eur J Biochem. 1991 Mar 14;196(2):261-9
Authors: Graham HC, Williams RJ, Littlechild...