2nrm

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{{STRUCTURE_2nrm| PDB=2nrm | SCENE= }}
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'''S-nitrosylated blackfin tuna myoglobin'''
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===S-nitrosylated blackfin tuna myoglobin===
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==Overview==
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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.
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==About this Structure==
==About this Structure==
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[[Category: S-nitrosylation]]
[[Category: S-nitrosylation]]
[[Category: Transport protein]]
[[Category: Transport protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 09:49:26 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 20:00:23 2008''

Revision as of 17:00, 27 July 2008

Image:2nrm.png

Template:STRUCTURE 2nrm

S-nitrosylated blackfin tuna myoglobin

Template:ABSTRACT PUBMED 17488722

About this Structure

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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