1f0v | pdb_00001f0v
Crystal structure of an Rnase A dimer displaying a new type of 3D domain swapping
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| 1f0v, resolution 1.7Å | |||||||||||||
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| Ligands: | DC, DG, GOL, PO4 | ||||||||||||
| Activity: | Pancreatic ribonuclease, with EC number 3.1.27.5 | ||||||||||||
| Related: | 1a2w
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
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. 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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