{"entry": {"accession": "MF7000767", "general": {"name": "Catechol 1,2 dioxygenase, mutant L69A (Acinetobacter radioresistens)", "pdb_id": "2xsv", "exp_method": "X-ray", "resolution": "1.80", "assembly": "Homodimer", "source_organism": "Acinetobacter radioresistens", "publication": {"pmid": "20869471", "authors": "Micalella C, Martignon S, Bruno S, Pioselli B, Caglio R, Valetti F, Pessione E, Giunta C, Rizzi M", "title": "X-ray crystallography, mass spectrometry and single crystal microspectrophotometry: a multidisciplinary characterization of catechol 1,2 dioxygenase.", "journal": "Biochim. Biophys. Acta", "year": "2011", "issue": "6", "volume": "1814", "pages": "817-23", "abstract": "Intradiol-cleaving catechol 1,2 dioxygenases are Fe(III) dependent enzymes that act on catechol and substituted catechols, including chlorocatechols pollutants, by inserting molecular oxygen in the aromatic ring. Members of this class are the object of intense biochemical investigations aimed at the understanding of their catalytic mechanism, particularly for designing mutants with selected catalytic properties. We report here an in depth investigation of catechol 1,2 dioxygenase IsoB from Acinetobacter radioresistens LMG S13 and its A72G and L69A mutants. By applying a multidisciplinary approach that includes high resolution X-rays crystallography, mass spectrometry and single crystal microspectrophotometry, we characterised the phospholipid bound to the enzyme and provided a structural framework to understand the inversion of substrate specificity showed by the mutants. Our results might be of help for the rational design of enzyme mutants showing a biotechnologically relevant substrate specificity, particularly to be used in bioremediation. This article is part of a Special Issue entitled: Protein Structure and Function in the Crystalline State."}}, "function": {"molecular_function": {"go": [{"accession": "GO:0018576", "name": "catechol 1,2-dioxygenase activity"}, {"accession": "GO:0008199", "name": "ferric iron binding"}]}, "biological_process": {"go": [{"accession": "GO:0042952", "name": "beta-ketoadipate pathway"}, {"accession": "GO:0019614", "name": "catechol-containing compound catabolic 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": "catechol 1,2-dioxygenase", "source_organism": "Acinetobacter radioresistens", "uniprot": {"id": "Q9F103", "start": "2", "end": "306", "coverage": "99%", "sequence": "MNRQQIDALVKQMNVDTAKGPVDERIQQVVVRLLGDLFQAIEDLDIQPSEVWKGLEYLTDAGQANELGLLAAGLGLEHYLDLRADEADAKAGITGGTPRTIEGPLYVAGAPESVGFARMDDGSESDKVDTLIIEGTVTDTEGNIIEGAKVEVWHANSLGNYSFFDKSQSDFNLRRTILTDVNGKYVALTTMPVGYGCPPEGTTQALLNKLGRHGNRPSHVHYFVSAPGYRKLTTQFNIEGDEYLWDDFAFATRDGLVATATDVTDEAEIARRELDKPFKHITFNVELVKEAEAAPSSEVERRRASA", "length": "306"}, "regions": {"region": [{"region_type": "secondary structure", "region_name": "helix", "region_start": "8", "region_end": "21"}, {"region_type": "secondary structure", "region_name": "helix", "region_start": "29", "region_end": "50"}, {"region_type": "secondary structure", "region_name": "helix", "region_start": "53", "region_end": "70"}, {"region_type": "secondary structure", "region_name": "helix", "region_start": "72", "region_end": "80"}, {"region_type": "secondary structure", "region_name": "helix", "region_start": "81", "region_end": "97"}, {"region_type": "secondary structure", "region_name": "helix", "region_start": "207", "region_end": "216"}, {"region_type": "secondary structure", "region_name": "helix", "region_start": "271", "region_end": "278"}, {"region_type": "secondary structure", "region_name": "strand", "region_start": "113", "region_end": "114"}, {"region_type": "secondary structure", "region_name": "strand", "region_start": "118", "region_end": "120"}, {"region_type": "secondary structure", "region_name": "strand", "region_start": "122", "region_end": "124"}, {"region_type": "secondary structure", "region_name": "strand", "region_start": "136", "region_end": "144"}, {"region_type": "secondary structure", "region_name": "strand", "region_start": "155", "region_end": "159"}, {"region_type": "secondary structure", "region_name": "strand", "region_start": "180", "region_end": "184"}, {"region_type": "secondary structure", "region_name": "strand", "region_start": "190", "region_end": "196"}, {"region_type": "secondary structure", "region_name": "strand", "region_start": "201", "region_end": "202"}, {"region_type": "secondary structure", "region_name": "strand", "region_start": "221", "region_end": "222"}, {"region_type": "secondary structure", "region_name": "strand", "region_start": "225", "region_end": "231"}, {"region_type": "secondary structure", "region_name": "strand", "region_start": "238", "region_end": "244"}, {"region_type": "secondary structure", "region_name": "strand", "region_start": "263", "region_end": "264"}, {"region_type": "secondary structure", "region_name": "strand", "region_start": "267", "region_end": "269"}, {"region_type": "secondary structure", "region_name": "strand", "region_start": "284", "region_end": "288"}, {"region_type": "secondary structure", "region_name": "strand", "region_start": "291", "region_end": "292"}, {"region_type": "secondary structure", "region_name": "strand", "region_start": "310", "region_end": "311"}, {"region_type": "pfam", "region_id": "PF04444", "region_name": "Catechol dioxygenase N terminus", "region_start": "23", "region_end": "92"}]}}, {"id": "A-2", "name": "catechol 1,2-dioxygenase", "source_organism": "Acinetobacter radioresistens", "uniprot": {"id": "Q9F103", "start": "2", "end": "306", "coverage": "99%", "sequence": "MNRQQIDALVKQMNVDTAKGPVDERIQQVVVRLLGDLFQAIEDLDIQPSEVWKGLEYLTDAGQANELGLLAAGLGLEHYLDLRADEADAKAGITGGTPRTIEGPLYVAGAPESVGFARMDDGSESDKVDTLIIEGTVTDTEGNIIEGAKVEVWHANSLGNYSFFDKSQSDFNLRRTILTDVNGKYVALTTMPVGYGCPPEGTTQALLNKLGRHGNRPSHVHYFVSAPGYRKLTTQFNIEGDEYLWDDFAFATRDGLVATATDVTDEAEIARRELDKPFKHITFNVELVKEAEAAPSSEVERRRASA", "length": "306"}, "regions": {"region": {"region_type": "pfam", "region_id": "PF04444", "region_name": "Catechol dioxygenase N terminus", "region_start": "23", "region_end": "92"}}}]}, "evidence": {"evidence_level": "Indirect evidence", "evidence_coverage": "Only some parts of the structure participates in mutual synergistic folding.", "sequence_domain": "Dioxygenase", "complex_evidence": "A 'helical zipper', consisting of five N-terminal helices and one extending from the catalytic domain from each subunit forms the dimer interafce, termed linker domain. Helices 4 and 5 lie against the catalytic domain, and helix 4 even donates some residues to the active-site cavity (PMID:10801478).", "chain_evidence": [{"chain_id": "A", "support": "N/A"}, {"chain_id": "A-2", "support": "N/A"}]}, "related_structures": {"id": ["MF7000760", "MF7000761", "MF7000762", "MF7000763", "MF7000764", "MF7000765", "MF7000766", "MF7000767", "MF7000768", "MF7000769", "MF7000770", "MF7000771"]}}}