2jnv | pdb_00002jnv

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

spinqualitylabelsall models 2jnv, 20 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2jnv is a 1 chain structure with sequence from Orysa. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 1th5, 1veh Gene: NIFU1 (ORYSA) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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 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. The cooperative role of OsCnfU-1A domain I and domain II in the iron sulphur cluster transfer process as revealed by NMR.,Saio T, Kumeta H, Ogura K, Yokochi M, Asayama M, Katoh S, Katoh E, Teshima K, Inagaki F J Biochem. 2007 Jul;142(1):113-21. Epub 2007 Jun 1. PMID:17545250 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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