3GQU
Pyrococcus Horikoshii NOP5 RNA Binding Domain
Summary for 3GQU
| Entry DOI | 10.2210/pdb3gqu/pdb |
| Related | 3GQX |
| Descriptor | NOP5P PROTEIN, IODIDE ION (3 entities in total) |
| Functional Keywords | rna binding domain, rna binding protein |
| Biological source | Pyrococcus horikoshii More |
| Total number of polymer chains | 1 |
| Total formula weight | 20504.12 |
| Authors | Reyes, F.E.,Hardin, J.W.,Batey, R.T. (deposition date: 2009-03-24, release date: 2009-04-21, Last modification date: 2024-02-21) |
| Primary citation | Hardin, J.W.,Reyes, F.E.,Batey, R.T. Analysis of a Critical Interaction within the Archaeal Box C/D Small Ribonucleoprotein Complex J.Biol.Chem., 284:15317-15324, 2009 Cited by PubMed Abstract: In archaea and eukarya, box C/D ribonucleoprotein (RNP) complexes are responsible for 2'-O-methylation of tRNAs and rRNAs. The archaeal box C/D small RNP complex requires a small RNA component (sRNA) possessing Watson-Crick complementarity to the target RNA along with three proteins: L7Ae, Nop5p, and fibrillarin. Transfer of a methyl group from S-adenosylmethionine to the target RNA is performed by fibrillarin, which by itself has no affinity for the sRNA-target duplex. Instead, it is targeted to the site of methylation through association with Nop5p, which in turn binds to the L7Ae-sRNA complex. To understand how Nop5p serves as a bridge between the targeting and catalytic functions of the box C/D small RNP complex, we have employed alanine scanning to evaluate the interaction between the Pyrococcus horikoshii Nop5p domain and an L7Ae box C/D RNA complex. From these data, we were able to construct an isolated RNA-binding domain (Nop-RBD) that folds correctly as demonstrated by x-ray crystallography and binds to the L7Ae box C/D RNA complex with near wild type affinity. These data demonstrate that the Nop-RBD is an autonomously folding and functional module important for protein assembly in a number of complexes centered on the L7Ae-kinkturn RNP. PubMed: 19336398DOI: 10.1074/jbc.M901368200 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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