Gene Ontology annotation through association of InterPro records with GO terms
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Combined Automated Annotation using Multiple IEA Methods
Methionine-121 coordination determines metal specificity in unfolded Pseudomonas aeruginosa azurin.
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Azurin binds copper very tightly.
"Pseudomonas aeruginosa azurin binds copper so tightly that it remains bound even upon polypeptide unfolding."
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Zinc can replace copper in vitro without structural change.
"Copper can be substituted with zinc without change in protein structure"
Metal-binding loop length and not sequence dictates structure.
Probing the reactivity of different forms of azurin by flavin photoreduction.
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The H117G variant is reduced more slowly by photoreduced flavins than the WT protein.
"The reactivity of the H117G variant in the absence of external ligands appears to be 2.5-fold lower than the WT reactivity"
Isomorphic deactivation of a Pseudomonas aeruginosa oxidoreductase: The crystal structure of Ag(I) metallated azurin at 1.7 Å.
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Silver binds at the copper site of apo-azurin, giving a redox-inert protein.
"X-ray crystallography of the silver-modified protein reveals that silver binds to azurin at the traditional copper mediated active site with nearly identical geometry."
A Pseudomonas aeruginosa type VI secretion system regulated by CueR facilitates copper acquisition.