6cc2

Crystal Structure of CDC45 from Entamoeba histolytica

spinqualitylabelsall models 6cc2, resolution 1.66Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6cc2 is a 1 chain structure with sequence from Entamoeba histolytica. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.66Å Ligands: CL, CME, EDO, MSE, PEG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function C4LUI8_ENTH1 Publication Abstract from PubMed Cdc45 plays a critical role at the core of the eukaryotic DNA replisome, serving as an essential scaffolding component of the replicative helicase holoenzyme Cdc45-MCM-GINS (CMG) complex. A 1.66-A-resolution crystal structure of the full-length Cdc45 protein from Entamoeba histolytica shows a protein fold similar to that observed previously for human Cdc45 in its active conformation, featuring the overall disk-like monomer shape and intimate contacts between the N- and C-terminal DHH domains. However, the E. histolytica Cdc45 structure shows several unique features, including a distinct orientation of the C-terminal DHHA1 domain, concomitant disordering of the adjacent protruding alpha-helical segment implicated in DNA polymerase epsilon interactions, and a unique conformation of the GINS/Mcm5-binding loop. These structural observations collectively suggest the possibility that Cdc45 can sample multiple conformations corresponding to different functional states. We propose that such conformational switch of Cdc45 may allow regulation of protein-protein interactions important in DNA replication. Crystal Structure of Entamoeba histolytica Cdc45 Suggests a Conformational Switch that May Regulate DNA Replication.,Kurniawan F, Shi K, Kurahashi K, Bielinsky AK, Aihara H iScience. 2018 May 25;3:102-109. doi: 10.1016/j.isci.2018.04.011. PMID:29901028 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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