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JKMRS Volume 24, No 3, pp 86, Structural flexibility of Escher...
2020년 09월 20일 / 조회수: 136

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

 

 

* Address correspondence to: Jin Hae Kim, Department of New Biology, Daegu Gyeongbuk Institute of Science &Technology, Daegu 42988, Republic of Korea, Tel: 82-53-785-1770; E-mail: jinhaekim@dgist.ac.kr


 

첨부파일 04-JKMRS-JH_Kim.pdf