1th5
From Proteopedia
Solution structure of C-terminal domain of NifU-like protein from Oryza sativa
Structural highlights
FunctionNIFU1_ORYSJ Molecular scaffold for [Fe-S] cluster assembly of chloroplastic iron-sulfur proteins (By similarity). Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedNifU-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 alpha-beta sandwich structure containing two alpha helices located on one side of the beta-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. The NMR structure of the domain II of a chloroplastic NifU-like protein OsNifU1A.,Kumeta H, Ogura K, Asayama M, Katoh S, Katoh E, Teshima K, Inagaki F J Biomol NMR. 2007 Jun;38(2):161-4. Epub 2007 Apr 13. PMID:17431550[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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Categories: Large Structures | Oryza sativa | Asayama M | Inagaki F | Katoh E | Katoh S | Kumeta H | Ogura K
