2nx0
From Proteopedia
| Line 4: | Line 4: | ||
==Overview== | ==Overview== | ||
| - | S-nitrosylation is a post-translational protein modification that can | + | 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== | ==About this Structure== | ||
| Line 14: | Line 14: | ||
[[Category: Thunnus orientalis]] | [[Category: Thunnus orientalis]] | ||
[[Category: Bonaventura, J.]] | [[Category: Bonaventura, J.]] | ||
| - | [[Category: Montfort, W | + | [[Category: Montfort, W R.]] |
| - | [[Category: Rodriguez, M | + | [[Category: Rodriguez, M M.]] |
| - | [[Category: Schreiter, E | + | [[Category: Schreiter, E R.]] |
[[Category: Weichsel, A.]] | [[Category: Weichsel, A.]] | ||
[[Category: HEM]] | [[Category: HEM]] | ||
| Line 26: | Line 26: | ||
[[Category: no]] | [[Category: no]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:11:57 2008'' |
Revision as of 16:11, 21 February 2008
|
Ferrous nitrosyl blackfin tuna myoglobin
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
2NX0 is a Single protein structure of sequence from Thunnus orientalis with , and 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
Page seeded by OCA on Thu Feb 21 18:11:57 2008
Categories: Single protein | Thunnus orientalis | Bonaventura, J. | Montfort, W R. | Rodriguez, M M. | Schreiter, E R. | Weichsel, A. | HEM | NO | SO4 | Ferrous nitrosyl | Myoglobin | Nitric oxide | No
