Structural adaptation of a thermostable biotin-binding protein in a psychrophilic environment

Meir, A., Bayer, E. A. and Livnah, O. (2012) Structural adaptation of a thermostable biotin-binding protein in a psychrophilic environment. Journal of Biological Chemistry, 287(22), pp. 17951-17962. (doi: 10.1074/jbc.M112.357186) (PMID:22493427) (PMCID:PMC3365750)

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Shwanavidin is an avidin-like protein from the marine proteobactrium Shewanella denitrificans, which exhibits an innate dimeric structure while maintaining high affinity toward biotin. A unique residue (Phe-43) from the L3,4 loop and a distinctive disulfide bridge were shown to account for the high affinity toward biotin. Phe-43 emulates the function and position of the critical intermonomeric Trp that characterizes the tetrameric avidins but is lacking in shwanavidin. The 18 copies of the apo-monomer revealed distinctive snapshots of L3,4 and Phe-43, providing rare insight into loop flexibility, binding site accessibility, and psychrophilic adaptation. Nevertheless, as in all avidins, shwanavidin also displays high thermostability properties. The unique features of shwanavidin may provide a platform for the design of a long sought after monovalent form of avidin, which would be ideal for novel types of biotechnological application.

Item Type:Articles
Glasgow Author(s) Enlighten ID:Meir Ben Efraim, Dr Amit
Authors: Meir, A., Bayer, E. A., and Livnah, O.
College/School:College of Medical Veterinary and Life Sciences > School of Infection & Immunity > Centre for Virus Research
Journal Name:Journal of Biological Chemistry
Publisher:American Society for Biochemistry and Molecular Biology, Inc.
ISSN (Online):1083-351X
Published Online:05 April 2012
Copyright Holders:Copyright © 2012 ASBMB
First Published:First published in Journal of Biological Chemistry 287(22): 17951-17962
Publisher Policy:Reproduced under a Creative Commons License

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