2JNV
Solution structure of C-terminal domain of NifU-like protein from Oryza sativa
Summary for 2JNV
| Entry DOI | 10.2210/pdb2jnv/pdb |
| Related | 1TH5 1VEH |
| Descriptor | NifU-like protein 1, chloroplast (1 entity in total) |
| Functional Keywords | iron-sulfur cluster binding, program for rice genome reserch, structural genomics, nppsfa, national project on protein structural and functional analyses, riken structural genomics/proteomics initiative, rsgi, metal transport |
| Biological source | Oryza sativa (rice) |
| Cellular location | Plastid, chloroplast stroma (By similarity): Q84LK7 |
| Total number of polymer chains | 1 |
| Total formula weight | 9823.24 |
| Authors | Saio, T.,Ogura, K.,Kumeta, H.,Yokochi, M.,Katoh, S.,Katoh, E.,Inagaki, F.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (deposition date: 2007-02-06, release date: 2007-12-18, Last modification date: 2023-12-20) |
| Primary citation | Saio, T.,Kumeta, H.,Ogura, K.,Yokochi, M.,Asayama, M.,Katoh, S.,Katoh, E.,Teshima, K.,Inagaki, F. The cooperative role of OsCnfU-1A domain I and domain II in the iron sulphur cluster transfer process as revealed by NMR J.Biochem.(Tokyo), 142:113-121, 2007 Cited by PubMed Abstract: OsCnfU-1A is a chloroplast-type Nfu-like protein that consists of tandem repeats sharing high sequence homology. Domain I of this protein, but not domain II, has a C-X-X-C motif that is thought to assemble an iron-sulphur cluster. Herein we report the solution structure of OsCnfU-1A domain I (73-153). Although OsCnfU-1A domain I is structurally similar to OsCnfU-1A domain II (154-226), the electrostatic surface potential of the 2 domains differs. Domain I has an acidic surface, whereas that of domain II is predominantly basic. Chemical shift perturbation studies on OsCnfU-1A domain I and domain II with ferredoxin revealed negligible chemical shift changes in domain I, whereas much larger chemical shift changes were observed in domain II. The residues with larger chemical shift changes were located on the basic surface of domain II. Considering that ferredoxin is predominantly negatively charged, we propose the following hypothesis: First, an iron-sulphur cluster is assembled on domain I. Next, domain II interacts with the ferredoxin, thus tethering domain I close to the ferredoxin. Finally, domain I transfers the iron-sulphur cluster to the ferredoxin. Thus, domain II facilitates the efficient transfer of the iron-sulphur cluster from domain I to the ferredoxin. PubMed: 17545250DOI: 10.1093/jb/mvm120 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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