6hfg

Structure of the REC114 PH domainStructure of the REC114 PH domain

Structural highlights 6hfg is a 1 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [RE114_MOUSE] Required for DNA double-strand breaks (DSBs) formation in unsynapsed regions during meiotic recombination (PubMed:20551173, PubMed:27723721). Probably acts by forming a complex with IHO1/CCDC36 and MEI4, which activates DSBs formation in unsynapsed regions, an essential step to ensure completion of synapsis (PubMed:27723721). Publication Abstract from PubMed Programmed formation of DNA double-strand breaks (DSBs) initiates the meiotic homologous recombination pathway. This pathway is essential for proper chromosome segregation at the first meiotic division and fertility. Meiotic DSBs are catalyzed by Spo11. Several other proteins are essential for meiotic DSB formation, including three evolutionarily conserved proteins first identified in Saccharomyces cerevisiae (Mer2, Mei4, and Rec114). These three S. cerevisiae proteins and their mouse orthologs (IHO1, MEI4, and REC114) co-localize on the axes of meiotic chromosomes, and mouse IHO1 and MEI4 are essential for meiotic DSB formation. Here, we show that mouse Rec114 is required for meiotic DSB formation. Moreover, MEI4 forms a complex with REC114 and IHO1 in mouse spermatocytes, consistent with cytological observations. We then demonstrated in vitro the formation of a stable complex between REC114 C-terminal domain and MEI4 N-terminal domain. We further determine the structure of the REC114 N-terminal domain that revealed similarity with Pleckstrin homology domains. These analyses provide direct insights into the architecture of these essential components of the meiotic DSB machinery. Mouse REC114 is essential for meiotic DNA double-strand break formation and forms a complex with MEI4.,Kumar R, Oliver C, Brun C, Juarez-Martinez AB, Tarabay Y, Kadlec J, de Massy B Life Sci Alliance. 2018 Dec 10;1(6):e201800259. doi: 10.26508/lsa.201800259., eCollection 2018 Dec. PMID:30569039 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

spinqualitylabelsall models 6hfg, resolution 2.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image