1TH5

Solution structure of C-terminal domain of NifU-like protein from Oryza sativa

Summary for 1TH5

• Entry DOI: 10.2210/pdb1th5/pdb
• Related: 1Q48
• NMR Information: BMRB: 6247
• Descriptor: NifU1 (1 entity in total)
• Functional Keywords: iron-sulfur cluster binding, structural genomics, program for rice genome research, unknown function
• Biological source: Oryza sativa (rice)
• Cellular location: Plastid, chloroplast stroma (By similarity): Q84LK7
• Total number of polymer chains: 1
• Total formula weight: 8105.71

Authors

Kumeta, H.,Ogura, K.,Asayama, M.,Katoh, S.,Katoh, E.,Inagaki, F. (deposition date: 2004-06-01, release date: 2005-09-27, Last modification date: 2024-05-29)

Primary citation

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, 38:161-164, 2007

PubMed Abstract: 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.

PubMed: 17431550
DOI: 10.1007/s10858-007-9155-9

Experimental method

SOLUTION NMR