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2BB2

X-RAY ANALYSIS OF BETA B2-CRYSTALLIN AND EVOLUTION OF OLIGOMERIC LENS PROTEINS

Summary for 2BB2
Entry DOI10.2210/pdb2bb2/pdb
DescriptorBETA B2-CRYSTALLIN, BETA-MERCAPTOETHANOL (3 entities in total)
Functional Keywordseye lens protein
Biological sourceBos taurus (cattle)
Total number of polymer chains1
Total formula weight20897.27
Authors
Bax, B.,Lapatto, R.,Nalini, V.,Driessen, H.,Lindley, P.F.,Mahadevan, D.,Blundell, T.L.,Slingsby, C. (deposition date: 1992-09-21, release date: 1993-10-31, Last modification date: 2024-06-05)
Primary citationBax, B.,Lapatto, R.,Nalini, V.,Driessen, H.,Lindley, P.F.,Mahadevan, D.,Blundell, T.L.,Slingsby, C.
X-ray analysis of beta B2-crystallin and evolution of oligomeric lens proteins.
Nature, 347:776-780, 1990
Cited by
PubMed Abstract: The beta, gamma-crystallins form a class of homologous proteins in the eye lens. Each gamma-crystallin comprises four topologically equivalent, Greek key motifs; pairs of motifs are organized around a local dyad to give domains and two similar domains are in turn related by a further local dyad. Sequence comparisons and model building predicted that hetero-oligomeric beta-crystallins also had internally quadruplicated subunits, but with extensions at the N and C termini, indicating that beta, gamma-crystallins evolved in two duplication steps from an ancestral protein folded as a Greek key. We report here the X-ray analysis at 2.1 A resolution of beta B2-crystallin homodimer which shows that the connecting peptide is extended and the two domains separated in a way quite unlike gamma-crystallin. Domain interactions analogous to those within monomeric gamma-crystallin are intermolecular and related by a crystallographic dyad in the beta B2-crystallin dimer. This shows how oligomers can evolve by conserving an interface rather than connectivity. A further interaction between dimers suggests a model for more complex aggregates of beta-crystallin in the lens.
PubMed: 2234050
DOI: 10.1038/347776a0
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.1 Å)
Structure validation

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