6zd2

Structure of apo telomerase from Candida Tropicalis truncated from C-terminal domain

spinqualitylabelsall models 6zd2, resolution 2.84Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6zd2 is a 1 chain structure with sequence from Cantt. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: NA Gene: CTRG_04008 (CANTT) Activity: RNA-directed DNA polymerase, with EC number 2.7.7.49 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [C5MCQ7_CANTT] Telomerase is a ribonucleoprotein enzyme essential for the replication of chromosome termini in most eukaryotes. It elongates telomeres. It is a reverse transcriptase that adds simple sequence repeats to chromosome ends by copying a template sequence within the RNA component of the enzyme.[RuleBase:RU365061] Publication Abstract from PubMed Telomerase plays critical roles in cellular aging, in the emergence and/or development of cancer, and in the capacity for stem-cell renewal, consists of a catalytic telomerase reverse transcriptase (TERT) and a template-encoding RNA (TER). TERs from diverse organisms contain two conserved structural elements: the template-pseudoknot (T-PK) and a helical three-way junction (TWJ). Species-specific features of the structure and function of telomerase make obtaining a more in-depth understanding of the molecular mechanism of telomerase particularly important. Here, we report the first structural studies of N-terminally truncated TERTs from Candida albicans and Candida tropicalis in apo form and complexed with their respective TWJs in several conformations. We found that Candida TERT proteins perform only one round of telomere addition in the presence or absence of PK/TWJ and display standard reverse transcriptase activity. The C-terminal domain adopts at least two extreme conformations and undergoes conformational interconversion, which regulates the catalytic activity. Most importantly, we identified a conserved tertiary structural motif, called the U-motif, which interacts with the reverse transcriptase domain and is crucial for catalytic activity. Together these results shed new light on the structure and mechanics of fungal TERTs, which show common TERT characteristics, but also display species-specific features. Crystal structures of N-terminally truncated telomerase reverse transcriptase from fungidouble dagger.,Zhai LT, Rety S, Chen WF, Song ZY, Auguin D, Sun B, Dou SX, Xi XG Nucleic Acids Res. 2021 Apr 15. pii: 6226674. doi: 10.1093/nar/gkab261. PMID:33856462 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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