Database accession: MF7000767
Name: Catechol 1,2 dioxygenase, mutant L69A (Acinetobacter radioresistens)
PDB ID: 2xsv
Experimental method: X-ray (1.80 Å)
Assembly: Homodimer
Source organism: Acinetobacter radioresistens
Primary publication of the structure:
Micalella C, Martignon S, Bruno S, Pioselli B, Caglio R, Valetti F, Pessione E, Giunta C, Rizzi M
X-ray crystallography, mass spectrometry and single crystal microspectrophotometry: a multidisciplinary characterization of catechol 1,2 dioxygenase.
(2011) Biochim. Biophys. Acta 1814: 817-23
PMID: 20869471
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.
Annotations from the GeneOntology database. Only terms that fit at least two of the interacting proteins are shown. Molecular function:
catechol 1,2-dioxygenase activity catechol 1,2-dioxygenase activity
ferric iron binding ferric iron binding
Biological process:
beta-ketoadipate pathway beta-ketoadipate pathway
catechol-containing compound catabolic process catechol-containing compound catabolic process
Cellular component: not assigned
Structural annotations of the participating protein chains.Entry contents: 2 distinct polypeptide molecules
Chains: A, A-2
Notes: All chains according to the most probable oligomerization state stored in PDBe were considered.
Number of unique protein segments: 1
Name: catechol 1,2-dioxygenase
Source organism: Acinetobacter radioresistens
Length: 306 residues
Sequence:Sequence according to the corresponding UniProt protein segmentMNRQQIDALVKQMNVDTAKGPVDERIQQVVVRLLGDLFQAIEDLDIQPSEVWKGLEYLTDAGQANELGLLAAGLGLEHYLDLRADEADAKAGITGGTPRTIEGPLYVAGAPESVGFARMDDGSESDKVDTLIIEGTVTDTEGNIIEGAKVEVWHANSLGNYSFFDKSQSDFNLRRTILTDVNGKYVALTTMPVGYGCPPEGTTQALLNKLGRHGNRPSHVHYFVSAPGYRKLTTQFNIEGDEYLWDDFAFATRDGLVATATDVTDEAEIARRELDKPFKHITFNVELVKEAEAAPSSEVERRRASA
UniProtKB AC: Q9F103 (positions: 2-306)
Coverage: 99%
Name: catechol 1,2-dioxygenase
Source organism: Acinetobacter radioresistens
Length: 306 residues
Sequence:Sequence according to the corresponding UniProt protein segmentMNRQQIDALVKQMNVDTAKGPVDERIQQVVVRLLGDLFQAIEDLDIQPSEVWKGLEYLTDAGQANELGLLAAGLGLEHYLDLRADEADAKAGITGGTPRTIEGPLYVAGAPESVGFARMDDGSESDKVDTLIIEGTVTDTEGNIIEGAKVEVWHANSLGNYSFFDKSQSDFNLRRTILTDVNGKYVALTTMPVGYGCPPEGTTQALLNKLGRHGNRPSHVHYFVSAPGYRKLTTQFNIEGDEYLWDDFAFATRDGLVATATDVTDEAEIARRELDKPFKHITFNVELVKEAEAAPSSEVERRRASA
UniProtKB AC: Q9F103 (positions: 2-306)
Coverage: 99%
Evidence demonstrating that the participating proteins are unstructured prior to the interaction and their folding is coupled to binding. Representative domain in related structures: Dioxygenase
Evidence level: Indirect evidence
Evidence coverage: Only some parts of the structure participates in mutual synergistic folding.
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 A:
N/A
Chain A-2:
N/A
Surface and contacts features:
Structures from the PDB that contain the same number of proteins, and the proteins from the two structures show a sufficient degree of pairwise similarity, i.e. they belong to the same UniRef90 cluster (the full proteins exhibit at least 90% sequence identity) and convey roughly the same region to their respective interactions (the two regions from the two proteins share a minimum of 70% overlap). Download the CIF file (.cif)
Download this entry's XML file (.xml)
Download this entry's JSON file (.json)
