4CA9
Structure of the Nucleoplasmin-like N-terminal domain of Drosophila FKBP39
Summary for 4CA9
| Entry DOI | 10.2210/pdb4ca9/pdb |
| NMR Information | BMRB: 19541 |
| Descriptor | 39 KDA FK506-BINDING NUCLEAR PROTEIN (1 entity in total) |
| Functional Keywords | isomerase, proline isomerase, nucleoplasmin, histone chaperone |
| Biological source | DROSOPHILA MELANOGASTER (FRUIT FLY) |
| Total number of polymer chains | 5 |
| Total formula weight | 54102.05 |
| Authors | Artero, J.,Forsyth, T.,Callow, P.,Watson, A.A.,Zhang, W.,Laue, E.D.,Edlich-Muth, C.,Przewloka, M. (deposition date: 2013-10-07, release date: 2014-10-29, Last modification date: 2024-06-19) |
| Primary citation | Edlich-Muth, C.,Artero, J.,Callow, P.,Przewloka, M.R.,Watson, A.A.,Zhang, W.,Glover, D.M.,Debski, J.,Dadlez, M.,Round, A.R.,Trevor Forsyth, V.,Laue, E.D. The Pentameric Nucleoplasmin Fold is Present in Drosophila Fkbp39 and a Large Number of Chromatin-Related Proteins. J.Mol.Biol., 427:1949-, 2015 Cited by PubMed Abstract: Nucleoplasmin is a histone chaperone that consists of a pentameric N-terminal domain and an unstructured C-terminal tail. The pentameric core domain, a doughnut-like structure with a central pore, is only found in the nucleoplasmin family. Here, we report the first structure of a nucleoplasmin-like domain (NPL) from the unrelated Drosophila protein, FKBP39, and we present evidence that this protein associates with chromatin. Furthermore, we show that two other chromatin proteins, Arabidopsis thaliana histone deacetylase type 2 (HD2) and Saccharomyces cerevisiae Fpr4, share the NPL fold and form pentamers, or a dimer of pentamers in the case of HD2. Thus, we propose a new family of proteins that share the pentameric nucleoplasmin-like NPL domain and are found in protists, fungi, plants and animals. PubMed: 25813344DOI: 10.1016/J.JMB.2015.03.010 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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