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Literature summary for 4.6.1.18 extracted from

  • Pica, A.; Merlino, A.; Buell, A.K.; Knowles, T.P.; Pizzo, E.; DAlessio, G.; Sica, F.; Mazzarella, L.
    Three-dimensional domain swapping and supramolecular protein assembly: insights from the X-ray structure of a dimeric swapped variant of human pancreatic RNase (2013), Acta Crystallogr. Sect. D, 69, 2116-2123.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
enzyme as dimer and tetramer after three-dimensional domain swapping, hanging-drop vapour-diffusion method, mixing of 1.6 mg/ml protein in 0.1 M sodium citrate buffer, pH 6.5, and 0.3 M NaCl, with reservoir solution containing 22% w/v PEG 8000, 0.1 M ammonium sulfate, X-ray diffraction structure determination and analysis at 2.70 A resolution Homo sapiens

Protein Variants

Protein Variants Comment Organism
additional information deletion of five residues in the loop connecting the N-terminal helix to the core of monomeric human pancreatic ribonuclease leads to the formation of an enzymatically active domain-swapped dimer. Three-dimensional domain swapping can be a mechanism for the formation of elaborate large assemblies in which the protein, apart from the swapping, retains its original fold Homo sapiens

Metals/Ions

Metals/Ions Comment Organism Structure
sulfate 13 sulfate anions are identified in the electrondensity map of the two dimers in the asymmetric unit of the crystal, confirming that this ion plays a fundamental role in the crystallization process. Four sulfate ions are positioned at the active sites, as typically observed in several other members of the pancreatic-like superfamily, the remaining anions are located on positive patches of the rod surface Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens P07998
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-

Source Tissue

Source Tissue Comment Organism Textmining
pancreas
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Homo sapiens
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Subunits

Subunits Comment Organism
monomer
-
Homo sapiens
More deletion of five residues in the loop connecting the N-terminal helix to the core of monomeric human pancreatic ribonuclease leads to the formation of an enzymatically active domain-swapped dimer. Domain-swapped dimer fibrils can form in solution. Two dimers in the asymmetric unit of the crystal: twofold symmetry of the dimers with a very strong inter-dimer association, a composite active site is generated by residues belonging to subunits A and B of one of the two dimers in the asymmetric unit Homo sapiens

Synonyms

Synonyms Comment Organism
pancreatic RNase
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Homo sapiens