3MVD
Crystal structure of the chromatin factor RCC1 in complex with the nucleosome core particle
Summary for 3MVD
| Entry DOI | 10.2210/pdb3mvd/pdb |
| Related | 1KX5 1ZLA |
| Descriptor | Histone H3.2, Histone H4, Histone H2A, ... (7 entities in total) |
| Functional Keywords | protein-dna complex, nucleosome core particle (ncp), ncp-chromatin factor complex, 7-bladed beta-propeller, signaling protein-structural protein-dna complex, signaling protein/structural protein/dna |
| Biological source | Xenopus laevis (clawed frog,common platanna,platanna) More |
| Cellular location | Nucleus: P84233 P62799 P02281 P25171 Nucleus (By similarity): Q6AZJ8 |
| Total number of polymer chains | 12 |
| Total formula weight | 289622.04 |
| Authors | Makde, R.D.,England, J.R.,Yennawar, H.P.,Tan, S. (deposition date: 2010-05-04, release date: 2010-08-25, Last modification date: 2023-09-06) |
| Primary citation | Makde, R.D.,England, J.R.,Yennawar, H.P.,Tan, S. Structure of RCC1 chromatin factor bound to the nucleosome core particle. Nature, 467:562-566, 2010 Cited by PubMed Abstract: The small GTPase Ran enzyme regulates critical eukaryotic cellular functions including nuclear transport and mitosis through the creation of a RanGTP gradient around the chromosomes. This concentration gradient is created by the chromatin-bound RCC1 (regulator of chromosome condensation) protein, which recruits Ran to nucleosomes and activates Ran's nucleotide exchange activity. Although RCC1 has been shown to bind directly with the nucleosome, the molecular details of this interaction were not known. Here we determine the crystal structure of a complex of Drosophila RCC1 and the nucleosome core particle at 2.9 Å resolution, providing an atomic view of how a chromatin protein interacts with the histone and DNA components of the nucleosome. Our structure also suggests that the Widom 601 DNA positioning sequence present in the nucleosomes forms a 145-base-pair nucleosome core particle, not the expected canonical 147-base-pair particle. PubMed: 20739938DOI: 10.1038/nature09321 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.9 Å) |
Structure validation
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