Work

Characterization and crystallization of core streptavidin.

Year: 1987

Type: article

Abstract: We have characterized a streptavidin product that had been reduced to a minimal size that still retained full biotin-binding activity. This core streptavidin is proteolyzed at both ends at points that correspond closely with the termini of hen egg white avidin. Core streptavidin is more soluble than is the parent molecule. We have grown three different types of crystals of core streptavidin. The symmetry properties of these crystals prove that the molecule is a tetramer organized in tetrahedral (D2) point symmetry. The crystallographic response to the interaction of biotin with core streptavidin indicates that some conformational change accompanies ligand binding. We are attempting to determine the three-dimensional structure of streptavidin and its complex with selenobiotin from these crystals of core streptavidin.

Source: Journal of Biological Chemistry

DOI: 10.1016/s0021-9258(18)47884-2

Authors: A Pähler, W A Hendrickson, M A Kolks, C E Argaraña, C R Cantor

Institutions: Howard Hughes Medical Institute, Columbia University

Language: English

Topic: Biotin and Related Studies

Subfield: Cell Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: hybrid

Estimated APC paid: $3,430

Funders: National Cancer Institute, National Institute of General Medical Sciences