{"entry": {"accession": "MF7000842", "general": {"name": "Hydroperoxide resistance protein, OhrB (Bacillus subtilis)", "pdb_id": "2bjo", "exp_method": "X-ray", "resolution": "2.10", "assembly": "Homodimer", "source_organism": "Bacillus subtilis", "publication": {"pmid": "18084074", "authors": "Cooper DR, Surendranath Y, Devedjiev Y, Bielnicki J, Derewenda ZS", "title": "Structure of the Bacillus subtilis OhrB hydroperoxide-resistance protein in a fully oxidized state.", "journal": "Acta Crystallogr. D Biol. Crystallogr.", "year": "2007", "issue": "Pt 12", "volume": "63", "pages": "1269-73", "abstract": "The crystal structure of the fully oxidized form of the Bacillus subtilis organic hydroperoxide-resistance (OhrB) protein is reported at 2.1 A resolution. The electron density reveals an intact catalytic disulfide bond (Cys55-Cys119) in each of the two molecules, which are intertwined into a canonical obligate dimer. However, the stereochemistry of the disulfides is unorthodox and strained, suggesting that they are sensitive to reducing agents. A deep solvent-accessible gorge reaching Cys55 may represent the access route for the reductant."}}, "function": {"biological_process": {"go": {"accession": "GO:0006979", "name": "response to oxidative stress"}}}, "macromolecules": {"general": {"nr_of_chains": "2", "nr_of_unique_protein_segments": "1", "class": "Homooligomeric enzymes", "subclass": "Homodimeric enzymes", "note": "All chains according to the most probable oligomerization state stored in PDBe were considered."}, "chain": [{"id": "A", "name": "Organic hydroperoxide resistance protein OhrB", "source_organism": "Bacillus subtilis", "uniprot": {"id": "P80242", "start": "2", "end": "136", "coverage": "99%", "sequence": "MALFTAKVTARGGRAGHITSDDGVLDFDIVMPNAKKEGQTGTNPEQLFAAGYAACFGGALEHVAKEQNIEIDSEIEGQVSLMKDESDGGFKIGVTLVVNTKDLDREKAQELVNAAHEFCPYSKATRGNVDVKLELK", "length": "136"}, "regions": {"region": [{"region_type": "secondary structure", "region_name": "helix", "region_start": "13", "region_end": "15"}, {"region_type": "secondary structure", "region_name": "helix", "region_start": "43", "region_end": "66"}, {"region_type": "secondary structure", "region_name": "helix", "region_start": "104", "region_end": "119"}, {"region_type": "secondary structure", "region_name": "helix", "region_start": "119", "region_end": "126"}, {"region_type": "secondary structure", "region_name": "strand", "region_start": "4", "region_end": "11"}, {"region_type": "secondary structure", "region_name": "strand", "region_start": "17", "region_end": "20"}, {"region_type": "secondary structure", "region_name": "strand", "region_start": "26", "region_end": "28"}, {"region_type": "secondary structure", "region_name": "strand", "region_start": "74", "region_end": "84"}, {"region_type": "secondary structure", "region_name": "strand", "region_start": "89", "region_end": "99"}, {"region_type": "secondary structure", "region_name": "strand", "region_start": "132", "region_end": "136"}, {"region_type": "pfam", "region_id": "PF02566", "region_name": "OsmC-like protein", "region_start": "39", "region_end": "134"}]}}, {"id": "B", "name": "Organic hydroperoxide resistance protein OhrB", "source_organism": "Bacillus subtilis", "uniprot": {"id": "P80242", "start": "2", "end": "136", "coverage": "99%", "sequence": "MALFTAKVTARGGRAGHITSDDGVLDFDIVMPNAKKEGQTGTNPEQLFAAGYAACFGGALEHVAKEQNIEIDSEIEGQVSLMKDESDGGFKIGVTLVVNTKDLDREKAQELVNAAHEFCPYSKATRGNVDVKLELK", "length": "136"}, "regions": {"region": [{"region_type": "secondary structure", "region_name": "helix", "region_start": "31", "region_end": "35"}, {"region_type": "secondary structure", "region_name": "helix", "region_start": "43", "region_end": "67"}, {"region_type": "secondary structure", "region_name": "helix", "region_start": "104", "region_end": "119"}, {"region_type": "secondary structure", "region_name": "helix", "region_start": "119", "region_end": "126"}, {"region_type": "secondary structure", "region_name": "strand", "region_start": "4", "region_end": "11"}, {"region_type": "secondary structure", "region_name": "strand", "region_start": "17", "region_end": "20"}, {"region_type": "secondary structure", "region_name": "strand", "region_start": "26", "region_end": "28"}, {"region_type": "secondary structure", "region_name": "strand", "region_start": "73", "region_end": "84"}, {"region_type": "secondary structure", "region_name": "strand", "region_start": "89", "region_end": "100"}, {"region_type": "secondary structure", "region_name": "strand", "region_start": "131", "region_end": "136"}, {"region_type": "pfam", "region_id": "PF02566", "region_name": "OsmC-like protein", "region_start": "39", "region_end": "134"}]}}]}, "evidence": {"evidence_level": "Direct evidence", "evidence_coverage": "The full structure participates in mutual synergistic folding.", "sequence_domain": "OsmC-like protein", "complex_evidence": "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\u2013helix packing interactions of two long helices at the center of the hydrophobic core of the dimeric enzyme. Also, each \u03b2-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 \u03b2-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).", "chain_evidence": [{"chain_id": "A", "support": "N/A"}, {"chain_id": "B", "support": "N/A"}]}, "related_structures": {"id": ["MF7000837", "MF7000838", "MF7000839", "MF7000840", "MF7000841", "MF7000842", "MF7000843"]}}}