MF7000838 Hydroperoxide resistance protein (Deinococcus radiodurans) 1usp X-ray 1.9 Homodimer Deinococcus radiodurans 15054099 Meunier-Jamin C, Kapp U, Leonard GA, McSweeney S J. Biol. Chem. 2004 24 279 25830-7 GO:0006979 response to oxidative stress 2 1 Homooligomeric enzymes Homodimeric enzymes All chains according to the most probable oligomerization state stored in PDBe were considered. A Organic hydroperoxide resistance protein Deinococcus radiodurans Q9RTA8 3 139 98% MANVYTAEATATGGRAGTTRSSDDRLNLDLSVPAEMGGDGGPGTNPEQLFAAGYAACFQGALGVVSRRQKIDVPADSTITARVGLQKAGLAFALDVELEGHFPGLSREQAEGLMHAAHEVCPYSAATRNNVDVRLKVRE 139 secondary structure helix 33 37 secondary structure helix 45 69 secondary structure helix 106 121 secondary structure helix 121 128 secondary structure strand 5 12 secondary structure strand 18 21 secondary structure strand 27 29 secondary structure strand 78 88 secondary structure strand 91 101 secondary structure strand 134 137 pfam PF02566 OsmC-like protein 40 135 B Organic hydroperoxide resistance protein Deinococcus radiodurans Q9RTA8 2 139 99% MANVYTAEATATGGRAGTTRSSDDRLNLDLSVPAEMGGDGGPGTNPEQLFAAGYAACFQGALGVVSRRQKIDVPADSTITARVGLQKAGLAFALDVELEGHFPGLSREQAEGLMHAAHEVCPYSAATRNNVDVRLKVRE 139 pfam PF02566 OsmC-like protein 40 135 Direct evidence The full structure participates in mutual synergistic folding. OsmC-like protein Ohr is a tightly folded homodimer with a large buried hydrophobic surface area. The two monomers are tightly wrapped around each other in a head-to-tail orientation. Dimerization is dominated by helix–helix packing interactions of two long helices at the center of the hydrophobic core of the dimeric enzyme. Also, each β-sheet is composed of six strands, three from one monomer and three from the other (beta sheet augmentation). The hydrophobic core, as well as the surrounding β-sheets, are generated by combining elements of both monomers, therefore, it is clear that the two polypeptide chains have to fold together to form active Ohr, and that each monomer would individually be unstable. The two active sites are also located at the dimer interface (PMID:12485986). A N/A B N/A MF7000837 MF7000838 MF7000839 MF7000840 MF7000841 MF7000842 MF7000843