{"entry": {"accession": "MF7000869", "general": {"name": "Human ALR, mutant C142/145S", "pdb_id": "3u2m", "exp_method": "X-ray", "resolution": "2.00", "assembly": "Homodimer", "source_organism": "Homo sapiens", "publication": {"pmid": "22224850", "authors": "Banci L, Bertini I, Calderone V, Cefaro C, Ciofi-Baffoni S, Gallo A, Tokatlidis K", "title": "An electron-transfer path through an extended disulfide relay system: the case of the redox protein ALR.", "journal": "J. Am. Chem. Soc.", "year": "2012", "issue": "3", "volume": "134", "pages": "1442-5", "abstract": "The oxidative folding mechanism in the intermembrane space of human mitochondria underpins a disulfide relay system consisting of the import receptor Mia40 and the homodimeric FAD-dependent thiol oxidase ALR. The flavoprotein ALR receives two electrons per subunit from Mia40, which are then donated through one-electron reactions to two cytochrome c molecules, thus mediating a switch from two-electron to one-electron transfer. We dissect here the mechanism of the electron flux within ALR, characterizing at the atomic level the ALR intermediates that allow electrons to rapidly flow to cytochrome c. The intermediate critical for the electron-transfer process implies the formation of a specific inter-subunit disulfide which exclusively allows electron flow from Mia40 to FAD. This finding allows us to present a complete model for the electron-transfer pathway in ALR."}}, "function": {"molecular_function": {"go": [{"accession": "GO:0050660", "name": "flavin adenine dinucleotide binding"}, {"accession": "GO:0016971", "name": "flavin-dependent sulfhydryl oxidase activity"}, {"accession": "GO:0008083", "name": "growth factor activity"}, {"accession": "GO:0015035", "name": "protein-disulfide reductase activity"}]}, "cellular_component": {"go": [{"accession": "GO:0005829", "name": "cytosol"}, {"accession": "GO:0005615", "name": "extracellular space"}, {"accession": "GO:0005758", "name": "mitochondrial intermembrane space"}, {"accession": "GO:0005739", "name": "mitochondrion"}]}, "biological_process": {"go": [{"accession": "GO:0072717", "name": "cellular response to actinomycin D"}, {"accession": "GO:0071222", "name": "cellular response to lipopolysaccharide"}, {"accession": "GO:0097237", "name": "cellular response to toxic substance"}, {"accession": "GO:0071356", "name": "cellular response to tumor necrosis factor"}, {"accession": "GO:0001889", "name": "liver development"}, {"accession": "GO:0097421", "name": "liver regeneration"}, {"accession": "GO:0043066", "name": "negative regulation of apoptotic process"}, {"accession": "GO:0045953", "name": "negative regulation of natural killer cell mediated cytotoxicity"}, {"accession": "GO:2000573", "name": "positive regulation of DNA biosynthetic process"}]}}, "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": "FAD-linked sulfhydryl oxidase ALR", "source_organism": "Homo sapiens", "uniprot": {"id": "P55789", "start": "91", "end": "205", "coverage": "56%", "sequence": "MAAPGERGRFHGGNLFFLPGGARSEMMDDLATDARGRGAGRRDAAASASTPAQAPTSDSPVAEDASRRRPCRACVDFKTWMRTQQKRDTKFREDCPPDREELGRHSWAVLHTLAAYYPDLPTPEQQQDMAQFIHLFSKFYPCEECAEDLRKRLCRNHPDTRTRACFTQWLCHLHNEVNRKLGKPDFDCSKVDERWRDGWKDGSCD", "length": "205"}, "regions": {"region": [{"region_type": "secondary structure", "region_name": "helix", "region_start": "8", "region_end": "27"}, {"region_type": "secondary structure", "region_name": "helix", "region_start": "32", "region_end": "50"}, {"region_type": "secondary structure", "region_name": "helix", "region_start": "52", "region_end": "65"}, {"region_type": "secondary structure", "region_name": "helix", "region_start": "72", "region_end": "91"}, {"region_type": "secondary structure", "region_name": "helix", "region_start": "97", "region_end": "99"}, {"region_type": "secondary structure", "region_name": "helix", "region_start": "100", "region_end": "106"}, {"region_type": "pfam", "region_id": "PF04777", "region_name": "Erv1 / Alr family", "region_start": "104", "region_end": "196"}]}}, {"id": "A-2", "name": "FAD-linked sulfhydryl oxidase ALR", "source_organism": "Homo sapiens", "uniprot": {"id": "P55789", "start": "91", "end": "205", "coverage": "56%", "sequence": "MAAPGERGRFHGGNLFFLPGGARSEMMDDLATDARGRGAGRRDAAASASTPAQAPTSDSPVAEDASRRRPCRACVDFKTWMRTQQKRDTKFREDCPPDREELGRHSWAVLHTLAAYYPDLPTPEQQQDMAQFIHLFSKFYPCEECAEDLRKRLCRNHPDTRTRACFTQWLCHLHNEVNRKLGKPDFDCSKVDERWRDGWKDGSCD", "length": "205"}, "regions": {"region": {"region_type": "pfam", "region_id": "PF04777", "region_name": "Erv1 / Alr family", "region_start": "104", "region_end": "196"}}}]}, "evidence": {"evidence_level": "Insufficient evidence (candidate)", "evidence_coverage": "The full structure participates in mutual synergistic folding.", "sequence_domain": "ERV/ALR sulfhydryl oxidase domain", "complex_evidence": "There is no information on the stability/disorder of the monomeric forms of FAD-linked sulfhydryl oxidases. The wild-type protein is a dimer in solution (analytical equilibrium ultracentrifugation) (PMID:19576902). The, large, hydrophobic interface is made up of two longer, nearly antiparallel helices per monomer that mediate helix packing interactions to form the interface.", "chain_evidence": [{"chain_id": "A", "support": "N/A"}, {"chain_id": "A-2", "support": "N/A"}]}, "related_structures": {"id": ["MF7000866", "MF7000270", "MF7000867", "MF7000868", "MF7000869", "MF7000870"]}}}