6r2f

Crystal structure of TEX12 F102A F109E V116A in an alternative conformation

spinqualitylabelsall models 6r2f, resolution 2.29Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6r2f is a 4 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.29Å Ligands: CL, MPD Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function TEX12_HUMAN Publication Abstract from PubMed 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. Coiled-coil structure of meiosis protein TEX12 and conformational regulation by its C-terminal tip.,Dunce JM, Salmon LJ, Davies OR Commun Biol. 2022 Sep 7;5(1):921. doi: 10.1038/s42003-022-03886-9. PMID:36071143 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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