1F0V

Crystal structure of an Rnase A dimer displaying a new type of 3D domain swapping

Summary for 1F0V

• Entry DOI: 10.2210/pdb1f0v/pdb
• Related: 1a2w
• Descriptor: 5'-D(*CP*G)-3', RIBONUCLEASE A, PHOSPHATE ION, ... (5 entities in total)
• Functional Keywords: domain swapping, crystal, ribonuclease, bovine pancreas, hydrolase-dna complex, hydrolase/dna
• Biological source: Bos taurus (cattle)
• Cellular location: Secreted: P61823
• Total number of polymer chains: 8
• Total formula weight: 59717.16

Authors

Liu, Y.S.,Gotte, G.,Libonati, M.,Eisenberg, D.S. (deposition date: 2000-05-17, release date: 2001-02-21, Last modification date: 2024-11-20)

Primary citation

Liu, Y.S.,Gotte, G.,Libonati, M.,Eisenberg, D.S.
A domain-swapped RNase A dimer with implications for amyloid formation
Nat.Struct.Biol., 8:211-214, 2001

PubMed Abstract: Bovine pancreatic ribonuclease (RNase A) forms two types of dimers (a major and a minor component) upon concentration in mild acid. These two dimers exhibit different biophysical and biochemical properties. Earlier we reported that the minor dimer forms by swapping its N-terminal alpha-helix with that of an identical molecule. Here we find that the major dimer forms by swapping its C-terminal beta-strand, thus revealing the first example of three-dimensional (3D) domain swapping taking place in different parts of the same protein. This feature permits RNase A to form tightly bonded higher oligomers. The hinge loop of the major dimer, connecting the swapped beta-strand to the protein core, resembles a short segment of the polar zipper proposed by Perutz and suggests a model for aggregate formation by 3D domain swapping with a polar zipper.

PubMed: 11224563
DOI: 10.1038/84941

Experimental method

X-RAY DIFFRACTION (1.7 Å)