{"entry": {"accession": "MF7000843", "general": {"name": "Hydroperoxide resistance protein (Burkholderia pseudomallei)", "pdb_id": "6uhw", "exp_method": "NMR", "assembly": "Homodimer", "source_organism": "Burkholderia pseudomallei", "publication": {"pmid": "19888681", "authors": "Buchko GW, Hewitt SN, Napuli AJ, Van Voorhis WC, Myler PJ", "title": "Backbone and side chain (1)H, (13)C, and (15)N NMR assignments for the organic hydroperoxide resistance protein (Ohr) from Burkholderia pseudomallei.", "journal": "Biomol NMR Assign", "year": "2009", "issue": "2", "volume": "3", "pages": "163-6", "abstract": "Burkholderia pseudomallei is a NIAID Category B microorganism responsible for melioidosis. Here we report backbone and side chain NMR assignments for the 139-residue, homodimeric, organic hydroperoxide resistance protein (Ohr) from this organism."}}, "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", "source_organism": "Burkholderia pseudomallei", "uniprot": {"id": "Q3JK82", "start": "1", "end": "139", "coverage": "100%", "sequence": "MNILYKTAATSTGGRDGRATSHDQKLDVKLSAPRELGGAGAEGTNPEQLFAAGYSACFLSAMKFVAGQNKQTLPADTTVTAEVGIGPNEEGGFALDVELRVALPGLDAAAAKTLVDRAHHVCPYSNATRNNVAVRLVVA", "length": "139"}, "regions": {"region": [{"region_type": "secondary structure", "region_name": "helix", "region_start": "33", "region_end": "38"}, {"region_type": "secondary structure", "region_name": "helix", "region_start": "45", "region_end": "69"}, {"region_type": "secondary structure", "region_name": "helix", "region_start": "107", "region_end": "122"}, {"region_type": "secondary structure", "region_name": "helix", "region_start": "126", "region_end": "131"}, {"region_type": "secondary structure", "region_name": "strand", "region_start": "5", "region_end": "12"}, {"region_type": "secondary structure", "region_name": "strand", "region_start": "17", "region_end": "21"}, {"region_type": "secondary structure", "region_name": "strand", "region_start": "26", "region_end": "30"}, {"region_type": "secondary structure", "region_name": "strand", "region_start": "78", "region_end": "87"}, {"region_type": "secondary structure", "region_name": "strand", "region_start": "93", "region_end": "102"}, {"region_type": "secondary structure", "region_name": "strand", "region_start": "133", "region_end": "139"}, {"region_type": "pfam", "region_id": "PF02566", "region_name": "OsmC-like protein", "region_start": "41", "region_end": "136"}]}}, {"id": "B", "name": "Organic hydroperoxide resistance protein", "source_organism": "Burkholderia pseudomallei", "uniprot": {"id": "Q3JK82", "start": "1", "end": "139", "coverage": "100%", "sequence": "MNILYKTAATSTGGRDGRATSHDQKLDVKLSAPRELGGAGAEGTNPEQLFAAGYSACFLSAMKFVAGQNKQTLPADTTVTAEVGIGPNEEGGFALDVELRVALPGLDAAAAKTLVDRAHHVCPYSNATRNNVAVRLVVA", "length": "139"}, "regions": {"region": [{"region_type": "secondary structure", "region_name": "helix", "region_start": "45", "region_end": "70"}, {"region_type": "secondary structure", "region_name": "helix", "region_start": "107", "region_end": "122"}, {"region_type": "secondary structure", "region_name": "helix", "region_start": "124", "region_end": "130"}, {"region_type": "secondary structure", "region_name": "strand", "region_start": "5", "region_end": "12"}, {"region_type": "secondary structure", "region_name": "strand", "region_start": "17", "region_end": "21"}, {"region_type": "secondary structure", "region_name": "strand", "region_start": "26", "region_end": "30"}, {"region_type": "secondary structure", "region_name": "strand", "region_start": "78", "region_end": "87"}, {"region_type": "secondary structure", "region_name": "strand", "region_start": "93", "region_end": "102"}, {"region_type": "secondary structure", "region_name": "strand", "region_start": "134", "region_end": "138"}, {"region_type": "pfam", "region_id": "PF02566", "region_name": "OsmC-like protein", "region_start": "41", "region_end": "136"}]}}]}, "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"]}}}