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Structural flexibility of Escherichia coli IscU, the iron-sulfur cluster scaffold protein

Title
Structural flexibility of Escherichia coli IscU, the iron-sulfur cluster scaffold protein
Authors
Kim, BokyungKim, Jin Hae
DGIST Authors
Kim, Bokyung; Kim, Jin Hae
Issue Date
2020-09
Citation
Journal of the Korean Magnetic Resonance Society, 24(3), 86-90
Type
Article
Article Type
Article
Author Keywords
NMR spectroscopyiron-sulfur clusteriron-sulfur cluster biogenesisprotein structureprotein dynamics
ISSN
1226-6531
Abstract
Iron-sulfur (Fe-S) clusters are one of the most ancient yet essential cofactors mediating various essential biological processes. In prokaryotes, Fe-S clusters are generated via several distinctive biogenesis mechanisms, among which the ISC (Iron-Sulfur Cluster) mechanism plays a house-keeping role to satisfy cellular needs for Fe-S clusters. The Escherichia coli ISC mechanism is maintained by several essential protein factors, whose structural characterization has been of great interest to reveal mechanistic details of the Fe-S cluster biogenesis mechanisms. In particular, nuclear magnetic resonance (NMR) spectroscopic approaches have contributed much to elucidate dynamic features not only in the structural states of the protein components but also in the interaction between them. The present minireview discusses recent advances in elucidating structural features of IscU, the key player in the E. coli ISC mechanism. IscU accommodates exceptional structural flexibility for its versatile activities, for which NMR spectroscopy was particularly successful. We expect that understanding to the structural diversity of IscU provides critical insight to appreciate functional versatility of the Fe-S cluster biogenesis mechanism.
URI
http://hdl.handle.net/20.500.11750/12715
DOI
10.6564/JKMRS.2020.24.3.086
Publisher
한국자기공명학회
Related Researcher
Files:
There are no files associated with this item.
Collection:
Department of New BiologyProtein Structure Aging Laboratory1. Journal Articles


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