Cytochrome c 552 from the thermophilic bacterium Hydrogenobacter thermophilus is a typical c-type cytochrome which binds heme covalently via two thioether bonds between the two heme vinyl groups and two cysteine thiol groups in a CXXCH sequence motif. This protein was converted to a b-type cytochrome by substitution of the two cysteine residues by alanines (Tomlinson and Ferguson in Proc Natl Acad Sci USA 97:5156â??5160, 2000a). To probe the significance of the covalent attachment of the heme in the c-type protein, 15N relaxation and hydrogen exchange studies have been performed for the wild-type and b-type proteins. The two variants share very similar backbone dynamic properties, both proteins showing high 15N order parameters in the four main helices, with reduced values in an exposed loop region (residues 18â??21), and at the C-terminal residue Lys80. Some subtle changes in chemical shift and hydrogen exchange protection are seen between the wild-type and b-type variant proteins, not only for residues at and neighbouring the mutation sites, but also for some residues in the heme binding pocket. Overall, the results suggest that the main role of the covalent linkages between the heme group and the protein chain must be to increase the stability of the protein.
Comparison of backbone dynamics of the type III antifreeze protein and antifreeze-like domain of human sialic acid synthase
Comparison of backbone dynamics of the type III antifreeze protein and antifreeze-like domain of human sialic acid synthase
Abstract
Antifreeze proteins (AFPs) are found in a variety of cold-adapted (psychrophilic) organisms to promote survival at subzero temperatures by binding to ice crystals and decreasing the freezing temperature of body fluids. The type III AFPs are small globular proteins that consist of one α-helix, three 310-helices, and two β-strands. Sialic acids play important roles in a variety of biological functions, such as...
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NMR structure and dynamics of recombinant wild type and mutated jerdostatin, a selective inhibitor of integrin ?(1) ?(1).
NMR structure and dynamics of recombinant wild type and mutated jerdostatin, a selective inhibitor of integrin ?(1) ?(1).
NMR structure and dynamics of recombinant wild type and mutated jerdostatin, a selective inhibitor of integrin ?(1) ?(1).
Proteins. 2011 May 10;
Authors: Carbajo RJ, Sanz L, Mosulén S, Pérez A, Marcinkiewicz C, Pineda-Lucena A, Calvete JJ
NMR analysis of four recombinant jerdostatin molecules was assessed to define the structural basis of two naturally occurring gain-of-function events: C-terminal dipeptide processing and...
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[NMR paper] Probing the sweet determinants of brazzein: wild-type brazzein and a tasteless variant, brazzein-ins(R18a-I18b), exhibit different pH-dependent NMR chemical shifts.
Probing the sweet determinants of brazzein: wild-type brazzein and a tasteless variant, brazzein-ins(R18a-I18b), exhibit different pH-dependent NMR chemical shifts.
Related Articles Probing the sweet determinants of brazzein: wild-type brazzein and a tasteless variant, brazzein-ins(R18a-I18b), exhibit different pH-dependent NMR chemical shifts.
Biochem Biophys Res Commun. 2005 Sep 16;335(1):256-63
Authors: Zhao Q, Song J, Jin Z, Danilova V, Hellekant G, Markley JL
Brazzein is a small, intensely sweet protein. As a probe of the functional...
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[NMR paper] NMR analysis shows that a b-type variant of Hydrogenobacter thermophilus cytochrome c
NMR analysis shows that a b-type variant of Hydrogenobacter thermophilus cytochrome c552 retains its native structure.
Related Articles NMR analysis shows that a b-type variant of Hydrogenobacter thermophilus cytochrome c552 retains its native structure.
J Biol Chem. 2004 Apr 9;279(15):15177-82
Authors: Wain R, Redfield C, Ferguson SJ, Smith LJ
Conversion of Hydrogenobacter thermophilus cytochrome c(552) into a b-type cytochrome by mutagenesis of both heme-binding cysteines to alanines significantly reduces the stability of the protein...
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[NMR paper] Dynamics of tryptophan binding to Escherichia coli Trp repressor wild type and AV77 m
Dynamics of tryptophan binding to Escherichia coli Trp repressor wild type and AV77 mutant: an NMR study.
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Biochemistry. 1995 Oct 10;34(40):13183-9
Authors: Schmitt TH, Zheng Z, Jardetzky O
Binding of L-tryptophan to Escherichia coli trp repressor wild type (WT) and AV77 mutant was studied by 1H NMR spectroscopy. Ligand binding to the proteins resulted in changes in line widths and chemical shifts of ligand resonances, but...
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[NMR paper] 13C NMR and fluorescence analysis of tryptophan dynamics in wild-type and two single-
13C NMR and fluorescence analysis of tryptophan dynamics in wild-type and two single-Trp variants of Escherichia coli thioredoxin.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-cellhub.gif http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles 13C NMR and fluorescence analysis of tryptophan dynamics in wild-type and two single-Trp variants of Escherichia coli thioredoxin.
Biophys J. 1994 Jun;66(6):2111-26
Authors: Kemple MD, Yuan...
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[NMR paper] 13C NMR and fluorescence analysis of tryptophan dynamics in wild-type and two single-
13C NMR and fluorescence analysis of tryptophan dynamics in wild-type and two single-Trp variants of Escherichia coli thioredoxin.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-cellhub.gif http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles 13C NMR and fluorescence analysis of tryptophan dynamics in wild-type and two single-Trp variants of Escherichia coli thioredoxin.
Biophys J. 1994 Jun;66(6):2111-26
Authors: Kemple MD, Yuan...
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[NMR paper] Comparative proton NMR analysis of wild-type cytochrome c peroxidase from yeast, the
Comparative proton NMR analysis of wild-type cytochrome c peroxidase from yeast, the recombinant enzyme from Escherichia coli, and an Asp-235----Asn-235 mutant.
Related Articles Comparative proton NMR analysis of wild-type cytochrome c peroxidase from yeast, the recombinant enzyme from Escherichia coli, and an Asp-235----Asn-235 mutant.
Biochemistry. 1990 Sep 18;29(37):8797-804
Authors: Satterlee JD, Erman JE, Mauro JM, Kraut J
Proton NMR spectra of cytochrome c peroxidase (CcP) isolated from yeast (wild type) and two Escherichia coli...
Comparison of the backbone dynamics of wild-type Hydrogenobacter thermophilus cytochrome c 552 and its b -type variant
Linear Mode
