S-Nitrosylation-induced conformational change in blackfin tuna myoglobin

Eric R. Schreiter, María M. Rodríguez, Andrzej Weichsel, William "Bill" Montfort, Joseph Bonaventura

Research output: Contribution to journalArticle

46 Citations (Scopus)

Abstract

S-Nitrosylation is a post-translational protein modification that can alter the function of a variety of proteins. Despite the growing wealth of information that this modification may have important functional consequences, little is known about the structure of the moiety or its effect on protein tertiary structure. Here we report high-resolution x-ray crystal structures of S-nitrosylated and unmodified blackfin tuna myoglobin, which demonstrate that in vitro S-nitrosylation of this protein at the surface-exposed Cys-10 directly causes a reversible conformational change by "wedging" apart a helix and loop. Furthermore, we have demonstrated in solution and in a single crystal that reduction of the S-nitrosylated myoglobin with dithionite results in NO cleavage from the sulfur of Cys-10 and rebinding to the reduced heme iron, showing the reversibility of both the modification and the conformational changes. Finally, we report the 0.95-Å structure of ferrous nitrosyl myoglobin, which provides an accurate structural view of the NO coordination geometry in the context of a globin heme pocket.

Original languageEnglish (US)
Pages (from-to)19773-19780
Number of pages8
JournalJournal of Biological Chemistry
Volume282
Issue number27
DOIs
StatePublished - Jul 6 2007

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Tuna
Myoglobin
Heme
Dithionite
Proteins
Globins
Protein S
Post Translational Protein Processing
Tertiary Protein Structure
Sulfur
Membrane Proteins
Iron
Crystal structure
X-Rays
Single crystals
X rays
Geometry

ASJC Scopus subject areas

  • Biochemistry

Cite this

S-Nitrosylation-induced conformational change in blackfin tuna myoglobin. / Schreiter, Eric R.; Rodríguez, María M.; Weichsel, Andrzej; Montfort, William "Bill"; Bonaventura, Joseph.

In: Journal of Biological Chemistry, Vol. 282, No. 27, 06.07.2007, p. 19773-19780.

Research output: Contribution to journalArticle

Schreiter, ER, Rodríguez, MM, Weichsel, A, Montfort, WB & Bonaventura, J 2007, 'S-Nitrosylation-induced conformational change in blackfin tuna myoglobin', Journal of Biological Chemistry, vol. 282, no. 27, pp. 19773-19780. https://doi.org/10.1074/jbc.M701363200
Schreiter, Eric R. ; Rodríguez, María M. ; Weichsel, Andrzej ; Montfort, William "Bill" ; Bonaventura, Joseph. / S-Nitrosylation-induced conformational change in blackfin tuna myoglobin. In: Journal of Biological Chemistry. 2007 ; Vol. 282, No. 27. pp. 19773-19780.
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AU - Rodríguez, María M.

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AU - Bonaventura, Joseph

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AB - S-Nitrosylation is a post-translational protein modification that can alter the function of a variety of proteins. Despite the growing wealth of information that this modification may have important functional consequences, little is known about the structure of the moiety or its effect on protein tertiary structure. Here we report high-resolution x-ray crystal structures of S-nitrosylated and unmodified blackfin tuna myoglobin, which demonstrate that in vitro S-nitrosylation of this protein at the surface-exposed Cys-10 directly causes a reversible conformational change by "wedging" apart a helix and loop. Furthermore, we have demonstrated in solution and in a single crystal that reduction of the S-nitrosylated myoglobin with dithionite results in NO cleavage from the sulfur of Cys-10 and rebinding to the reduced heme iron, showing the reversibility of both the modification and the conformational changes. Finally, we report the 0.95-Å structure of ferrous nitrosyl myoglobin, which provides an accurate structural view of the NO coordination geometry in the context of a globin heme pocket.

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