Related ArticlesStructural rearrangements of the two domains of Azotobacter vinelandii rhodanese upon sulfane sulfur release: essential molecular dynamics, 15N NMR relaxation and deuterium exchange on the uniformly labeled protein.
Int J Biol Macromol. 2003 Dec;33(4-5):193-201
Authors: Cicero DO, Melino S, Orsale M, Brancato G, Amadei A, Forlani F, Pagani S, Paci M
The Azotobacter vinelandii rhodanese is a 31kDa sulfurtransferase protein that catalyzes the transfer of sulfur atom from thiosulfate to cyanide in the detoxification process from cyanide and is able to insert sulfur atom in the iron-sulfur cluster. A study of the uniformly 15N isotopic labeling by high resolution NMR, before obtaining the backbone sequential assignment, has been carried out. The sulfur loaded and the sulfur discharged forms of the enzyme show very similar HSQC spectra with a good spectral dispersion. Few resonances show changes in chemical shift between the two forms. Relaxation parameters T(1), T(2) and 1H-15N NOE of all amide nitrogen atoms, as well as isotope exchange kinetics, show that the two forms exhibit the same global correlation time and hydrodynamic properties. In parallel, essential dynamics studies show that formation and discharging of catalytic cysteine persulfide group has no significant impact on the overall conformation of the protein. These results, taken together, give a clearcut answer to the question if the catalytic mechanism of the enzyme involves a change in the conformation and/or in the mutual orientation of the two domains. On the contrary these results clearly indicate that upon the catalytic mechanism the two domains of the protein behave as a unique fold.
NMR spectroscopy with the stringent substrate rhodanese bound to the single-ring variant SR1 of the E. coli chaperonin GroEL.
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Protein Sci. 2011 Jun 1;
Authors: Koculi E, Horst R, Horwich AL, Wüthrich K
NMR observation of the uniformly (2) H,(15) N-labeled stringent 33 kDa substrate protein rhodanese in a productive complex with the uniformly (14) N-labeled 400 kDa single-ring version of the E. coli chaperonin GroEL, SR1,...
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[NMR paper] NMR structural comparison of the cytoplasmic juxtamembrane domains of G-protein-coupl
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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] NMR analysis of the binding of a rhodanese peptide to a minichaperone in solution.
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J Mol Biol. 1999 Sep 10;292(1):181-90
Authors: Kobayashi N, Freund SM, Chatellier J, Zahn R, Fersht AR
A detailed structural analysis of interactions between denatured proteins and GroEL is essential for an understanding of its mechanism. Minichaperones constitute an excellent paradigm for obtaining high-resolution structural information about the binding site and...
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Protein Eng. 1998 Nov;11(11):957-9
Authors: Whiteman P, Downing AK, Handford PA
Fibrillin-1 is a modular glycoprotein and a major component of the 10-12 nm microfibrils of the extracellular matrix. Mutations in the fibrillin-1 (FBN 1) gene result in the connective tissue disease the...
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J Biol Chem. 2010 Nov 12;
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G protein-activated inwardly rectifying potassium channel (GIRK) plays crucial roles in regulating heart...
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[NMR paper] NMR studies of Azotobacter vinelandii and Pseudomonas putida seven-iron ferredoxins.
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J Biol Chem. 1992 Apr 25;267(12):8073-80
Authors: Cheng H, Grohmann K, Sweeney W
Ferredoxins are...
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J Biol Chem. 1990 Jul 25;265(21):12388-92
Authors: Cheng H, Grohmann K, Sweeney W
Pseudomonas putida and Azotobacter vinelandii ferredoxins each contain one cluster and one cluster. Their polypeptide chains are nearly identical, differing by only 15 residues out of a total of 106. T1...
Structural rearrangements of the two domains of Azotobacter vinelandii rhodanese upon
Linear Mode
