2nrm | pdb_00002nrm
S-nitrosylated blackfin tuna myoglobin
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Overview
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.
About this Structure
2NRM is a Protein complex structure of sequences from Thunnus atlanticus with HEM and GOL as ligands. Full crystallographic information is available from OCA.
Reference
S-nitrosylation-induced conformational change in blackfin tuna myoglobin., Schreiter ER, Rodriguez MM, Weichsel A, Montfort WR, Bonaventura J, J Biol Chem. 2007 Jul 6;282(27):19773-80. Epub 2007 May 8. PMID:17488722
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