2JX2
Solution conformation of RNA-bound NELF-E RRM
Summary for 2JX2
| Entry DOI | 10.2210/pdb2jx2/pdb |
| NMR Information | BMRB: 15543 |
| Descriptor | Negative elongation factor E (1 entity in total) |
| Functional Keywords | nelfe-rrm, coiled coil, nucleus, phosphorylation, repressor, rna-binding, transcription, transcription regulation, ubl conjugation |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 1 |
| Total formula weight | 13384.09 |
| Authors | Jampani, N.,Schweimer, K.,Wenzel, S.,Woehrl, B.M.,Roesch, P. (deposition date: 2007-11-02, release date: 2008-04-08, Last modification date: 2024-05-08) |
| Primary citation | Rao, J.N.,Schweimer, K.,Wenzel, S.,Wohrl, B.M.,Rosch, P. NELF-E RRM Undergoes Major Structural Changes in Flexible Protein Regions on Target RNA Binding Biochemistry, 47:3756-3761, 2008 Cited by PubMed Abstract: The E subunit of the human heterotetrameric negative transcription elongation factor (NELF-E) contains a canonical betaalphabetabetaalphabeta RNA recognition motif (RRM) that binds to a wide variety of RNA sequences. These induce very similar conformational changes in the RRM as determined by nuclear magnetic resonance spectroscopy. Although the RNA binding interface of a canonical RRM is mainly located at its beta-sheet surface, for NELF-E RRM large chemical shift perturbations are observed for residues in the flexible C-terminal region and the loop between beta 3 and alpha 2, and both regions are distant from the interface. We determined the solution structure of single-stranded transactivator responsive element (TAR) RNA-bound NELF-E RRM. This structure clearly shows that RNA binding to NELF-E RRM induces formation of a helix in the C-terminus. The RNA-bound form of NELF-E RRM is very similar to the RNA-bound form of U1A RRM, although the C-terminus of the NELF-E RRM is unstructured in the free protein, whereas it is helical in the U1A protein. Thus, RNA binding to NELF-E RRM induces a conformational change toward the U1A structure, resulting in highly similar RNA binding conformations for both proteins. PubMed: 18303858DOI: 10.1021/bi702429m PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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