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    azu azurin [ Pseudomonas aeruginosa PAO1 ]

    Gene ID: 878046, updated on 24-Aug-2024

    Summary

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    Gene symbol
    azu
    Gene description
    azurin
    Locus tag
    PA4922
    Gene type
    protein coding
    RefSeq status
    PROVISIONAL
    Organism
    Pseudomonas aeruginosa PAO1 (strain: PAO1)
    Lineage
    Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales; Pseudomonadaceae; Pseudomonas
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    Genomic context

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    Sequence:
    NC_002516.2 (5521664..5522110, complement)

    NC_002516.2Genomic Context describing neighboring genes Neighboring gene NAD synthetase Neighboring gene hypothetical protein Neighboring gene hypothetical protein Neighboring gene hypothetical protein

    Genomic regions, transcripts, and products

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    Genomic Sequence:
    NC_002516.2

    Go to nucleotide: Graphics FASTA GenBank

    Bibliography

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    Related articles in PubMed

    1. Enhancement of the Chaperone Activity of Alkyl Hydroperoxide Reductase C from Pseudomonas aeruginosa PAO1 Resulting from a Point-Specific Mutation Confers Heat Tolerance in Escherichia coli. Lee JT, et al. Mol Cells, 2016 Aug 31. PMID 27457208, Free PMC Article
    2. Methionine-121 coordination determines metal specificity in unfolded Pseudomonas aeruginosa azurin. Marks J, et al. J Biol Inorg Chem, 2004 Apr. PMID 14758526
    3. Conformational changes in azurin from Pseudomona aeruginosa induced through chemical and physical protocols. Fuentes L, et al. Biophys J, 2004 Sep. PMID 15345565, Free PMC Article
    4. Effects of a novel disulfide bond and engineered electrostatic interactions on the thermostability of azurin. Tigerström A, et al. Biochemistry, 2004 Oct 5. PMID 15449946
    5. The early steps in the unfolding of azurin. Rizzuti B, et al. Biochemistry, 2004 Dec 14. PMID 15581373

    See all (28) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. Review of activity of Pseudomonas aeruginosa azurin and azurin-like bacteriocins; including hijacking of key cellular regulators and cell surface receptors to remodel the cellular signaling networks.
      Title: Bacterial cupredoxin azurin hijacks cellular signaling networks: Protein-protein interactions and cancer therapy.
    2. this study shows that addition of Cys at position 78 modulates the functional shifting of this protein from a peroxidase to a chaperone
      Title: Enhancement of the Chaperone Activity of Alkyl Hydroperoxide Reductase C from Pseudomonas aeruginosa PAO1 Resulting from a Point-Specific Mutation Confers Heat Tolerance in Escherichia coli.
    3. Mercury metallation of the bacterial copper protein azurin is analogous to the one of human cerulopsmin and factor VIII in mercury poisoning.
      Title: Mercury metallation of the copper protein azurin and structural insight into possible heavy metal reactivity.
    4. Study presents the high-resolution (1.5 A) structure of azurin from Pseudomonas aeruginosa PAO1 spin labelled with MTSSL at position T21; due to the crystal-packing environment in the triclinic crystals, the label is observed in two different but fully ordered states.
      Title: High-resolution crystal structure of spin labelled (T21R1) azurin from Pseudomonas aeruginosa: a challenging structural benchmark for in silico spin labelling algorithms.
    5. Results suggest that a potential mechanism for the microbial toxicity of silver is the deactivation of copper oxidoreductases by the effective binding and structural mimicry by silver without the corresponding function.
      Title: Isomorphic deactivation of a Pseudomonas aeruginosa oxidoreductase: The crystal structure of Ag(I) metallated azurin at 1.7 Å.
    6. The study examines the spectral properties of tryptophan radicals in two azurin mutants (Az48W and ReAz108W).
      Title: Effects of the protein environment on the spectral properties of tryptophan radicals in Pseudomonas aeruginosa azurin.
    7. Atomic force spectroscopy was used to investigate the interaction of p28 peptide fragment of azurin with full-length p53 and its isolated domains at the single molecule level.
      Title: Interaction of an anticancer peptide fragment of azurin with p53 and its isolated domains studied by atomic force spectroscopy.
    8. structure of the active-site loop has a dramatic effect on the kinetic stability and the unfolding pathway
      Title: The influence of active site loop mutations on the thermal stability of azurin from Pseudomonas aeruginosa.
    9. Studies indicate that in the crystal structure of azurin the H20 is strongly hydrogen bonded to Y48 (2.7-2.8A tyrosine-O to histidine-N distance.
      Title: Redox properties of tyrosine and related molecules.
    10. Data show that almost all of the azurin variant potentials were shifted to higher values than WT azurin.
      Title: Reduction potential variations in azurin through secondary coordination sphere phenylalanine incorporations.
    Submit: New GeneRIF Correction See all GeneRIFs (17)

    General gene information

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    Homology

    Gene Ontology Provided by PseudoCAP

    Function Evidence Code Pubs
    enables copper ion binding IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    enables transition metal ion binding IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables zinc ion binding IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 

    General protein information

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    Preferred Names
    azurin
    NP_253609.1
    • Product name confidence: class 1 (Function experimentally demonstrated in P. aeruginosa)

    NCBI Reference Sequences (RefSeq)

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    Genome Annotation

    The following sections contain reference sequences that belong to a specific genome build. Explain

    Reference assembly

    Genomic

    1. NC_002516.2 Reference assembly

      Range
      5521664..5522110 complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NP_253609.1 azurin [Pseudomonas aeruginosa PAO1]

      See identical proteins and their annotated locations for NP_253609.1

      Status: PROVISIONAL

      UniProtKB/TrEMBL
      A0A4Y6GMG4
      Conserved Domains (1) summary
      COG3241
      Location:23 → 148
      COG3241; Azurin [Energy production and conversion]
    Nucleotide Protein
    Heading Accession and Version
    Protein Accession Links
    GenPept Link UniProtKB Link
    P00282.2

    Gene LinkOut

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