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spinqualitylabelsall models 1f0v, resolution 1.7Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

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

Overview

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.

About this Structure

1F0V is a Single protein structure of sequence from Bos taurus with PO4 and GOL as ligands. Active as Pancreatic ribonuclease, with EC number 3.1.27.5 Full crystallographic information is available from OCA.

Reference

A domain-swapped RNase A dimer with implications for amyloid formation., Liu Y, Gotte G, Libonati M, Eisenberg D, Nat Struct Biol. 2001 Mar;8(3):211-4. PMID:11224563

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