2nrm

S-nitrosylated blackfin tuna myoglobin

spinqualitylabelsall models 2nrm, resolution 1.09Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2nrm is a 1 chain structure with sequence from Thunnus atlanticus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.09Å Ligands: ACE, GOL, HEM, SNC Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function MYG_THUTH Monomeric heme protein which primary function is to store oxygen and facilitate its diffusion within muscle tissues. Reversibly binds oxygen through a pentacoordinated heme iron and enables its timely and efficient release as needed during periods of heightened demand. Depending on the oxidative conditions of tissues and cells, and in addition to its ability to bind oxygen, it also has a nitrite reductase activity whereby it regulates the production of bioactive nitric oxide. Under stress conditions, like hypoxia and anoxia, it also protects cells against reactive oxygen species thanks to its pseudoperoxidase activity.[UniProtKB:P02144] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Myoglobin 3D structures

Proteopedia Page Contributors and Editors (what is this?)

OCA