4A0I

Crystal structure of Survivin bound to the N-terminal tail of hSgo1

Summary for 4A0I

• Entry DOI: 10.2210/pdb4a0i/pdb
• Related: 1E31 1F3H 1XOX 4A0J 4A0N
• Descriptor: BACULOVIRAL IAP REPEAT-CONTAINING PROTEIN 5, SHUGOSHIN-LIKE 1, ZINC ION (3 entities in total)
• Functional Keywords: cell cycle, mitosis, cell division, chromosomal passenger complex, chromatin, centromere
• Biological source: HOMO SAPIENS (HUMAN); More
• Cellular location: Cytoplasm: O15392; Nucleus: Q5FBB7
• Total number of polymer chains: 4
• Total formula weight: 34175.74

Authors

Jeyaprakash, A.A.,Basquin, C.,Jayachandran, U.,Conti, E. (deposition date: 2011-09-09, release date: 2011-11-09, Last modification date: 2023-12-20)

Primary citation

Jeyaprakash, A.A.,Basquin, C.,Jayachandran, U.,Conti, E.
Structural Basis for the Recognition of Phosphorylated Histone H3 by the Survivin Subunit of the Chromosomal Passenger Complex.
Structure, 19:1625-, 2011

PubMed Abstract: Localization of the chromosomal passenger complex (CPC) at centromeres during early mitosis is essential for accurate chromosome segregation and is dependent on the phosphorylation of histone H3. We report the 2.7 Å resolution structure of the CPC subunit Survivin bound to the N-terminal tail of histone H3 carrying the Thr3 phosphorylation mark (Thr3ph). The BIR domain of Survivin recognizes the Ala1-Arg2-Thr3ph-Lys4 sequence, decoding the modification state and the free N terminus of histone H3 by a strategy similar to that used by PHD fingers. The structural analysis permitted the identification of putative Survivin-binding epitopes in other mitotic proteins, including human Shugoshin 1. Using biophysical and structural data, we show that a phospho-mimic N-terminal sequence such as that of hSgo1 (Ala1-Lys2-Glu3-Arg4) contains the specificity determinants to bind Survivin. Our findings suggest that the CPC engages in mutually exclusive interactions with other constituents of the mitotic machinery and a histone mark in chromatin.

PubMed: 22032967
DOI: 10.1016/J.STR.2011.09.002

Experimental method

X-RAY DIFFRACTION (2.605 Å)