8f9j | pdb_00008f9j

H64A swMb-PrNO adduct

spinqualitylabelsall models 8f9j, resolution 1.75Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8f9j is a 1 chain structure with sequence from Physeter catodon. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.75Å Ligands: HEM, SO4, XEM Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function MYG_PHYMC Serves as a reserve supply of oxygen and facilitates the movement of oxygen within muscles. Publication Abstract from PubMed Nitrosoalkanes (R-N horizontal lineO; R = alkyl) are biological intermediates that form from the oxidative metabolism of various amine (RNH(2)) drugs or from the reduction of nitroorganics (RNO(2)). RNO compounds bind to and inhibit various heme proteins. However, structural information on the resulting Fe-RNO moieties remains limited. We report the preparation of ferrous wild-type and H64A sw Mb(II)-RNO derivatives (lambda(max) 424 nm; R = Me, Et, Pr, iPr) from the reactions of Mb(III)-H(2)O with dithionite and nitroalkanes. The apparent extent of formation of the wt Mb derivatives followed the order MeNO > EtNO > PrNO > iPrNO, whereas the order was the opposite for the H64A derivatives. Ferricyanide oxidation of the Mb(II)-RNO derivatives resulted in the formation of the ferric Mb(III)-H(2)O precursors with loss of the RNO ligands. X-ray crystal structures of the wt Mb(II)-RNO derivatives at 1.76-2.0 A resoln. revealed N-binding of RNO to Fe and the presence of H-bonding interactions between the nitroso O-atoms and distal pocket His64. The nitroso O-atoms pointed in the general direction of the protein exterior, and the hydrophobic R groups pointed toward the protein interior. X-ray crystal structures for the H64A mutant derivatives were determined at 1.74-1.80 A resoln. An analysis of the distal pocket amino acid surface landscape provided an explanation for the differences in ligand orientations adopted by the EtNO and PrNO ligands in their wt and H64A structures. Our results provide a good baseline for the structural analysis of RNO binding to heme proteins possessing small distal pockets. Insights into Nitrosoalkane Binding to Myoglobin Provided by Crystallography of Wild-Type and Distal Pocket Mutant Derivatives.,Herrera VE, Charles TP, Scott TG, Prather KY, Nguyen NT, Sohl CD, Thomas LM, Richter-Addo GB Biochemistry. 2023 Apr 18;62(8):1406-1419. doi: 10.1021/acs.biochem.2c00725. Epub , 2023 Apr 3. PMID:37011611 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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