S-nitrosylation-induced conformational change in blackfin tuna myoglobin.

Published

Journal Article

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-A structure of ferrous nitrosyl myoglobin, which provides an accurate structural view of the NO coordination geometry in the context of a globin heme pocket.

Full Text

Duke Authors

Cited Authors

  • Schreiter, ER; Rodríguez, MM; Weichsel, A; Montfort, WR; Bonaventura, J

Published Date

  • July 2007

Published In

Volume / Issue

  • 282 / 27

Start / End Page

  • 19773 - 19780

PubMed ID

  • 17488722

Pubmed Central ID

  • 17488722

Electronic International Standard Serial Number (EISSN)

  • 1083-351X

International Standard Serial Number (ISSN)

  • 0021-9258

Digital Object Identifier (DOI)

  • 10.1074/jbc.m701363200

Language

  • eng