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Literature summary for 4.6.1.18 extracted from

  • Merlino, A.; Picone, D.; Ercole, C.; Balsamo, A.; Sica, F.
    Chain termini cross-talk in the swapping process of bovine pancreatic ribonuclease (2012), Biochimie, 94, 1108-1118.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
purified enzyme mutant P114A in monomeric and dimeric form, for the monomeric enzyme hanging drop vapour diffusion method is used mixing of 24 mg/ml protein with reservoir solution containing 35% w/v ammonium sulfate, 50% v/v of saturated NaCl, and 0.1 M acetate buffer, pH 6.6, 20°C, 1 week, for the dimeric enzyme sitting drop vapour diffusion method is used with 15 mg/ml protein mixed with precipitation solution containing 17-19% w/v PEG 20000, 0.1 M cacodylate buffer, pH 6.5, 100-150 mg/ml of trehalose, and 11 mM of 2'-deoxycytidylyl(3',5')-2'-deoxyguanosine, a few days, 20°C, X-ray diffraction structure determination and analysis at 2.10 A and 2.18 A resolution, respectively, molecular replacement Bos taurus

Protein Variants

Protein Variants Comment Organism
P114A site-directed mutagenesis, the mutation at the C-terminus affects the capability of the N-terminal alpha-helix to swap and the stability of both dimeric forms Bos taurus

Organism

Organism UniProt Comment Textmining
Bos taurus P61823
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-

Source Tissue

Source Tissue Comment Organism Textmining

Subunits

Subunits Comment Organism
dimer dimerization of the P114A mutant enzyme is dimerization is carried out through lyophilization from 40% acetic acid, the mutant efficiently oligomerizes under these conditions, the dimers are separated by gel filtration and ion exchange chromatography Bos taurus
monomer
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Bos taurus
More bovine pancreatic ribonuclease is able to swap the N-terminal alpha-helix (residues 1-13) and/or the C-terminal beta-strand (residues 116-124), forming a variety of oligomers, including two different dimers. Cis-trans isomerization of the Asn113-Pro114 peptide group is observed when the protein formed the C-terminal swapped dimer. Importance of the hydration shell in determining the cross-talk between the chain termini in the swapping process of RNase A Bos taurus

Synonyms

Synonyms Comment Organism
RNase A
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Bos taurus

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
45 66 thermal denaturation temperatures Tm of enzyme mutant P114A, wild-type enzyme RNase A, and N- and C-swapped dimers of the two proteins, overview Bos taurus

General Information

General Information Comment Organism
additional information the enzyme performs 3D domain swapping, a process by which two or more protein molecules exchange part of their structure to form intertwined dimers or higher oligomers Bos taurus