6HK9

Crystal structure of TEX12 F102A F109E V116A

6HK9 の概要

• エントリーDOI: 10.2210/pdb6hk9/pdb
• 関連するPDBエントリー: 6HK8
• 分子名称: Testis-expressed protein 12, CALCIUM ION, ACETATE ION, ... (5 entities in total)
• 機能のキーワード: synaptonemal complex, meiosis, recombination, coiled-coil, self-assembly, tex12, structural protein
• 由来する生物種: Homo sapiens (Human)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 18479.01

構造登録者

Dunce, J.M.,Salmon, L.J.,Davies, O.R. (登録日: 2018-09-06, 公開日: 2019-09-18, 最終更新日: 2024-12-04)

主引用文献

Dunce, J.M.,Salmon, L.J.,Davies, O.R.
Coiled-coil structure of meiosis protein TEX12 and conformational regulation by its C-terminal tip.
Commun Biol, 5:921-921, 2022

PubMed Abstract: Meiosis protein TEX12 is an essential component of the synaptonemal complex (SC), which mediates homologous chromosome synapsis. It is also recruited to centrosomes in meiosis, and aberrantly in certain cancers, leading to centrosome dysfunction. Within the SC, TEX12 forms an intertwined complex with SYCE2 that undergoes fibrous assembly, driven by TEX12's C-terminal tip. However, we hitherto lack structural information regarding SYCE2-independent functions of TEX12. Here, we report X-ray crystal structures of TEX12 mutants in three distinct conformations, and utilise solution light and X-ray scattering to determine its wild-type dimeric four-helical coiled-coil structure. TEX12 undergoes conformational change upon C-terminal tip mutations, indicating that the sequence responsible for driving SYCE2-TEX12 assembly within the SC also controls the oligomeric state and conformation of isolated TEX12. Our findings provide the structural basis for SYCE2-independent roles of TEX12, including the possible regulation of SC assembly, and its known functions in meiotic centrosomes and cancer.

PubMed: 36071143
DOI: 10.1038/s42003-022-03886-9

実験手法

X-RAY DIFFRACTION (1.454 Å)