1bd7

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Image:1bd7.gif

1bd7, resolution 2.78Å

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CIRCULARLY PERMUTED BB2-CRYSTALLIN

Overview

The betagamma-crystallins form a superfamily of eye lens proteins, comprised of multiple Greek motifs that are symmetrically organized into, domains and higher assemblies. In the betaB2-crystallin dimer each, polypeptide folds into two similar domains that are related to monomeric, gamma-crystallin by domain swapping. The crystal structure of the, circularly permuted two-domain betaB2 polypeptide shows that permutation, converts intermolecular domain pairing into intramolecular pairing., However, the dimeric permuted protein is, in fact, half a native tetramer., This result shows how the sequential order of domains in multi-domain, proteins can affect quaternary domain assembly.

About this Structure

1BD7 is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.

Reference

Circular permutation of betaB2-crystallin changes the hierarchy of domain assembly., Wright G, Basak AK, Wieligmann K, Mayr EM, Slingsby C, Protein Sci. 1998 Jun;7(6):1280-5. PMID:9655330

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