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High-resolution Crystal Structure of an Avidin-related Protein: Insight Into High-affinity Biotin Binding and Protein Stability by Yael Eisenberg-Domovich; Vesa P. Hytönen; Meir Wilchek; Edward A. Bayer; Markku S. Kulomaa; Oded Livnah is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

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The chicken avidin gene belongs to an extended gene family encoding seven avidin-related genes (AVRs), of which only avidin is expressed in the chicken. The sequences of AVR4 and AVR5 are identical and the common protein (AVR4) has been expressed both in insect and bacterial systems. The recombinant proteins are similarly hyperthermostable and bind biotin with similarly high affinities. AVR4 was crystallized in the apo and biotin-complexed forms and their structures were determined at high resolution. Its tertiary and quaternary structures are very similar to those of avidin and streptavidin. Its biotin-binding site shows only a few alterations compared with those of avidin and streptavidin, which account for the observed differences in binding affinities. The increased hyperthermostability can be attributed to the conformation of the critical L3,4 loop and the extensive network of 1-3 inter-monomeric interactions. The loop contains a tandem Pro-Gly sequence and an Asp-Arg ion pair that collectively induce rigidity, thus maintaining its closed and ordered conformation in both the apo and biotincomplexed forms. In addition, Tyr115 is present on the AVR4 1-3 monomer-monomer interface

Who reads High-resolution Crystal Structure of an Avidin-related Protein: Insight Into High-affinity Biotin Binding and Protein Stability?

Author

Yael Eisenberg-Domovich; Vesa P. Hytönen; Meir Wilchek; Edward A. Bayer; Markku S. Kulomaa; Oded Livnah

Publisher

International Union of Crystallography; Blackwell Publishing Inc.; International Union of Crystallography (IUCr) (ISSN 0907-4449)

Published

2005

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)