The NMR structure of the domain II of a chloroplastic NifU-like protein OsNifU1A

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• 作者：Hiroyuki Kumeta ; Kenji Ogura ; Munehiko Asayama ; Shizue Katoh ; Etsuko Katoh ; Keizo Teshima and Fuyuhiko Inagaki
• 关键词：Oryza sativa ; NifU ; NifU ; like protein ; Fe– ; S cluster ; NMR structure
• 刊名：Journal of Biomolecular NMR
• 出版年：2007
• 出版时间：June, 2007
• 年：2007
• 卷：38
• 期：2
• 页码：161-164
• 全文大小：372 KB

文摘

NifU-like proteins are a highly conserved protein that serves as the scaffold for assembly of Fe-S clusters. Chloroplastic NifU-like proteins have tandem NifU like domains, named domain I and domain II. Although the amino acid sequences of these domains are very similar to each other, the predicted functional region for the Fe-S cluster assembly, the CXXC motif, exists only in domain I. The structure of the domain II of chloroplastic NifU-like protein OsNifU1A has an α-β sandwich structure containing two α helices located on one side of the β-sheet. The electrostatic surface potential of OsNifU1A domain II is predominantly positively charged. Chloroplastic NifU-like proteins are targeted to ferredoxin for transferring the Fe-S cluster. The ferredoxin presents an overall negatively charged surface, which may evoke an electrostatic association with OsNifU1A domain II.