Crystallization (Comment) | Organism |
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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 | 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 | UniProt | Comment | Textmining |
---|---|---|---|
Bos taurus | P61823 | - |
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Source Tissue | Comment | Organism | Textmining |
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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 | - |
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 | Comment | Organism |
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RNase A | - |
Bos taurus |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
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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 | Comment | Organism |
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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 |