Summary information and primary citation
- PDB-id
-
3mvd;
SNAP-derived features in text and
JSON formats
- Class
- signaling protein-structural protein-DNA
- Method
- X-ray (2.9 Å)
- Summary
- Crystal structure of the chromatin factor rcc1 in
complex with the nucleosome core particle
- Reference
-
Makde RD, England JR, Yennawar HP, Tan S (2010):
"Structure
of RCC1 chromatin factor bound to the nucleosome core
particle." Nature, 467,
562-566. doi: 10.1038/nature09321.
- 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.
