JKMRS Volume 24, No 3, pp 86, Structural flexibility of Escher... | |
---|---|
2020년 09월 20일 / 조회수: 494 | |
Structural flexibility of Escherichia
coli IscU, the iron-sulfur cluster scaffold protein
Bokyung Kim and Jin Hae Kim*
Department of New Biology, Daegu Gyeongbuk Institute of
Science and Technology, Daegu 42988, Republic of Korea
Received Sep 15, 2020; Revised
Sep 18, 2020; Accepted Sep 18, 2020
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.
Keywords iron-sulfur cluster, iron-sulfur cluster biogenesis, protein structure, protein dynamics, NMR spectroscopy
|
|
첨부파일 | 04-JKMRS-JH_Kim.pdf |