2nrm
From Proteopedia
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| - | [[Image:2nrm.jpg|left|200px]] | + | [[Image:2nrm.jpg|left|200px]] |
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| - | '''S-nitrosylated blackfin tuna myoglobin''' | + | {{Structure |
| + | |PDB= 2nrm |SIZE=350|CAPTION= <scene name='initialview01'>2nrm</scene>, resolution 1.09Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene> and <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''S-nitrosylated blackfin tuna myoglobin''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2NRM is a [ | + | 2NRM is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Thunnus_atlanticus Thunnus atlanticus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NRM OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/17488722 17488722] |
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Thunnus atlanticus]] | [[Category: Thunnus atlanticus]] | ||
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[[Category: transport protein]] | [[Category: transport protein]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:50:08 2008'' |
Revision as of 15:50, 20 March 2008
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| , resolution 1.09Å | |||||||
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| Ligands: | and | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
S-nitrosylated 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
2NRM is a Protein complex structure of sequences from Thunnus atlanticus. 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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