1BD7

CIRCULARLY PERMUTED BB2-CRYSTALLIN

Summary for 1BD7

• Entry DOI: 10.2210/pdb1bd7/pdb
• Descriptor: CIRCULARLY PERMUTED BB2-CRYSTALLIN (2 entities in total)
• Functional Keywords: eye-lens protein, beta-crystallin b, multigene family
• Biological source: Rattus norvegicus (Norway rat)
• Total number of polymer chains: 2
• Total formula weight: 40306.85

Authors

Wright, G.,Basak, A.K.,Mayr, E.-M.,Glockshuber, R.,Slingsby, C. (deposition date: 1998-05-12, release date: 1998-10-21, Last modification date: 2024-04-03)

Primary citation

Wright, G.,Basak, A.K.,Wieligmann, K.,Mayr, E.M.,Slingsby, C.
Circular permutation of betaB2-crystallin changes the hierarchy of domain assembly.
Protein Sci., 7:1280-1285, 1998

PubMed Abstract: 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.

PubMed: 9655330

Experimental method

X-RAY DIFFRACTION (2.78 Å)