NDLI: The X-ray structure of a mutant eye lens beta B2-crystallin with truncated sequence extensions.

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The X-ray structure of a mutant eye lens beta B2-crystallin with truncated sequence extensions.

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The X-ray structure of a mutant eye lens beta B2-crystallin with truncated sequence extensions.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Slingsby, C. Trinkl, S. Jaenicke, R. Norledge, B. V.
Description	Country affiliation: United kingdom Author Affiliation: Norledge BV ( Birkbeck College, Department of Crystallography, London, United Kingdom.)
Abstract	beta-Crystallins are oligomeric eye lens proteins that are related to monomeric gamma-crystallins by domain swapping: like gamma-crystallins, they are comprised of two similar domains but they differ in having long sequence extensions. beta B2, a major component of beta-crystallin oligomers, self-associates to a homodimer in solution. In two crystal structures of native beta B2, the protein is a 222-symmetric tetramer of eight domains. It has previously been shown that a mutant of rat beta B2-crystallin, in which the bulk of the N- and C-terminal sequence extensions has been deleted, assembles into dimers and tetramers. Here we present the 3.0 A resolution X-ray structure of the tetramer, beta B2 delta NC1. The mutant tetramer has a very similar set of domain interactions to the native structure. However, the structures differ in the relative orientation of the two sets of four domains. The paired N- and C-terminal domain interface, which is at the heart of the dimer structure, is very similar to the native structure. However, the truncation of the C-terminal extension removes an important tryptophan residue, which prevents the extension from acting as a (non-covalent) linker, as it does in native beta B2. There is a knock-on structural effect that removes a contact between extension and covalent linker, and this appears to cause a small twist in the linker that is amplified into a 20 degrees rotation between sets of paired domains.
ISSN	09618368
e-ISSN	1469896X
Journal	Protein Science
Issue Number	8
Volume Number	6
Language	English
Publisher	Wiley-Blackwell (on behalf of The Protein Society)
Publisher Date	1997-08-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Crystallins Chemistry Amino Acid Sequence Animals Genetics Dimerization Molecular Sequence Data Mutagenesis X-ray Diffraction Research Support, Non-u.s. Gov't Discipline Biochemistry
Content Type	Text
Resource Type	Article
Subject	Medicine Molecular Biology Biochemistry

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