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Literature summary for 4.6.1.20 extracted from

  • Noguchi, S.
    Structural changes induced by the deamidation and isomerization of asparagine revealed by the crystal structure of Ustilago sphaerogena ribonuclease U2B (2010), Biopolymers, 93, 1003-1010.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
isoAsp containing ribonuclease U2B, hanging drop vapor diffusion method, 0.004 ml of 10 mg/ml protein in 50 mM sodium citrate, pH 4.5, containing 50 mM sodium chloride, are mixed with 0.004 ml of reservoir solution containing 0.84 M sodium dihydrogen phosphate and 1.26 M dipotassium hydrogen phosphate, pH 6.9, equilibration against 0.4 ml reservoir solution, 20°C, 2 days, X-ray diffraction structure determination and analysis at 1.32 A resolution Ustilago sphaerogena

Organism

Organism UniProt Comment Textmining
Ustilago sphaerogena P00654
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-

Purification (Commentary)

Purification (Comment) Organism
native RNase U2A by anion-exchange and 5'-adenylate aminohexyl affinity chromatography Ustilago sphaerogena

Subunits

Subunits Comment Organism
More formation of isoAsp32 induces a single turn unfolding of the alpha-helix from Asp29 to Asp34, and the region from Asp29 to Arg35 forms a U-shaped loop structure, overview Ustilago sphaerogena

Synonyms

Synonyms Comment Organism
ribonuclease U2B
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Ustilago sphaerogena

General Information

General Information Comment Organism
additional information formation of isoAsp32 induces a single turn unfolding of the alpha-helix from Asp29 to Asp34, and the region from Asp29 to Arg35 forms a U-shaped loop structure, overview. IsoAsp32 protrudes from the surface of the protein, and the abnormal beta-peptide bond in the main-chain and alpha-carboxylate in the side-chain is fully exposed. The structure suggests that the deamidation of the Asn and the isoAsp formation in proteins could confer immunogenicity Ustilago sphaerogena