3ESL
Crystal structure of the conserved N-terminal domain of the mitotic checkpoint component BUB1
Summary for 3ESL
Entry DOI | 10.2210/pdb3esl/pdb |
Descriptor | Checkpoint serine/threonine-protein kinase BUB1, 2-[N-CYCLOHEXYLAMINO]ETHANE SULFONIC ACID (3 entities in total) |
Functional Keywords | bub1, mitotic spindle checkpoint, tpr motif, all-alpha domain, mad3-like domain, chromosome instability, atp-binding, cell cycle, kinase, nucleotide-binding, nucleus, phosphorylation, serine/threonine-protein kinase, transferase, kinetochore localization, phosphoprotein |
Biological source | Saccharomyces cerevisiae (brewer's yeast,lager beer yeast,yeast) |
Cellular location | Nucleus: P41695 |
Total number of polymer chains | 2 |
Total formula weight | 49177.80 |
Authors | Bolanos-Garcia, V.M.,Chirgadze, D.Y.,Blundell, T.L. (deposition date: 2008-10-06, release date: 2009-02-17, Last modification date: 2023-12-27) |
Primary citation | Bolanos-Garcia, V.M.,Kiyomitsu, T.,D'Arcy, S.,Chirgadze, D.Y.,Grossmann, J.G.,Matak-Vinkovic, D.,Venkitaraman, A.R.,Yanagida, M.,Robinson, C.V.,Blundell, T.L. The Crystal Structure of the N-Terminal Region of BUB1 Provides Insight into the Mechanism of BUB1 Recruitment to Kinetochores. Structure, 17:105-116, 2009 Cited by PubMed Abstract: The interaction of the central mitotic checkpoint component BUB1 with the mitotic kinetochore protein Blinkin is required for the kinetochore localization and function of BUB1 in the mitotic spindle assembly checkpoint, the regulatory mechanism of the cell cycle that ensures the even distribution of chromosomes during the transition from metaphase to anaphase. Here, we report the 1.74 angstroms resolution crystal structure of the N-terminal region of BUB1. The structure is organized as a tandem arrangement of three divergent units of the tetratricopeptide motif. Functional assays in vivo of native and site-specific mutants identify the residues of human BUB1 important for the interaction with Blinkin and define one region of potential therapeutic interest. The structure provides insight into the molecular basis of Blinkin-specific recognition by BUB1 and, on a broader perspective, of the mechanism that mediates kinetochore localization of BUB1 in checkpoint-activated cells. PubMed: 19141287DOI: 10.1016/j.str.2008.10.015 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.74 Å) |
Structure validation
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