6IGX
Crystal structure of human CAP-G in complex with CAP-H
Summary for 6IGX
| Entry DOI | 10.2210/pdb6igx/pdb |
| Descriptor | Condensin complex subunit 3, Condensin complex subunit 2, 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID, ... (4 entities in total) |
| Functional Keywords | condensin i subunits, chromosome condensation, protein-protein interaction, heat repeats, cell cycle |
| Biological source | Homo sapiens (Human) More |
| Total number of polymer chains | 4 |
| Total formula weight | 202649.84 |
| Authors | Hara, K.,Migita, T.,Shimizu, K.,Hashimoto, H. (deposition date: 2018-09-26, release date: 2019-03-13, Last modification date: 2024-03-27) |
| Primary citation | Hara, K.,Kinoshita, K.,Migita, T.,Murakami, K.,Shimizu, K.,Takeuchi, K.,Hirano, T.,Hashimoto, H. Structural basis of HEAT-kleisin interactions in the human condensin I subcomplex. Embo Rep., 20:-, 2019 Cited by PubMed Abstract: Condensin I is a multi-protein complex that plays an essential role in mitotic chromosome assembly and segregation in eukaryotes. It is composed of five subunits: two SMC (SMC2 and SMC4), a kleisin (CAP-H), and two HEAT-repeat (CAP-D2 and CAP-G) subunits. Although balancing acts of the two HEAT-repeat subunits have been demonstrated to enable this complex to support the dynamic assembly of chromosomal axes in vertebrate cells, its underlying mechanisms remain poorly understood. Here, we report the crystal structure of a human condensin I subcomplex comprising hCAP-G and hCAP-H. hCAP-H binds to the concave surfaces of a harp-shaped HEAT-repeat domain of hCAP-G. Physical interaction between hCAP-G and hCAP-H is indeed essential for mitotic chromosome assembly recapitulated in egg cell-free extracts. Furthermore, this study reveals that the human CAP-G-H subcomplex has the ability to interact with not only double-stranded DNA, but also single-stranded DNA, suggesting functional divergence of the vertebrate condensin I complex in proper mitotic chromosome assembly. PubMed: 30858338DOI: 10.15252/embr.201847183 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.995 Å) |
Structure validation
Download full validation report
