Structural highlights
Function
[NIFU1_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 PubMed
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 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
- ↑ Kumeta H, Ogura K, Asayama M, Katoh S, Katoh E, Teshima K, Inagaki F. The NMR structure of the domain II of a chloroplastic NifU-like protein OsNifU1A. J Biomol NMR. 2007 Jun;38(2):161-4. Epub 2007 Apr 13. PMID:17431550 doi:10.1007/s10858-007-9155-9
