7NYQ
Crystal structure of the Mei-P26 NHL domain
Summary for 7NYQ
| Entry DOI | 10.2210/pdb7nyq/pdb |
| Descriptor | Meiotic P26, isoform C (2 entities in total) |
| Functional Keywords | mei-p26, nhl, rna recognition, trim-nhl proteins, rna binding protein |
| Biological source | Drosophila melanogaster (Fruit fly) |
| Total number of polymer chains | 2 |
| Total formula weight | 66587.99 |
| Authors | Salerno-Kochan, A.,Gaik, M.,Medenbach, J.,Glatt, S. (deposition date: 2021-03-23, release date: 2022-05-04, Last modification date: 2024-10-16) |
| Primary citation | Salerno-Kochan, A.,Horn, A.,Ghosh, P.,Nithin, C.,Koscielniak, A.,Meindl, A.,Strauss, D.,Krutyholowa, R.,Rossbach, O.,Bujnicki, J.M.,Gaik, M.,Medenbach, J.,Glatt, S. Molecular insights into RNA recognition and gene regulation by the TRIM-NHL protein Mei-P26. Life Sci Alliance, 5:-, 2022 Cited by PubMed Abstract: The TRIM-NHL protein Meiotic P26 (Mei-P26) acts as a regulator of cell fate in Its activity is critical for ovarian germline stem cell maintenance, differentiation of oocytes, and spermatogenesis. Mei-P26 functions as a post-transcriptional regulator of gene expression; however, the molecular details of how its NHL domain selectively recognizes and regulates its mRNA targets have remained elusive. Here, we present the crystal structure of the Mei-P26 NHL domain at 1.6 Å resolution and identify key amino acids that confer substrate specificity and distinguish Mei-P26 from closely related TRIM-NHL proteins. Furthermore, we identify mRNA targets of Mei-P26 in cultured cells and show that Mei-P26 can act as either a repressor or activator of gene expression on different RNA targets. Our work reveals the molecular basis of RNA recognition by Mei-P26 and the fundamental functional differences between otherwise very similar TRIM-NHL proteins. PubMed: 35512835DOI: 10.26508/lsa.202201418 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.6 Å) |
Structure validation
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