7cv1 | pdb_00007cv1

Structure of human tRNAHis guanylyltransferase (Thg1) in the presence of human mitochondrial tRNAHis

spinqualitylabelsall models 7cv1, resolution 4.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7cv1 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 4Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function THG1_HUMAN Adds a GMP to the 5'-end of tRNA(His) after transcription and RNase P cleavage. This step is essential for proper recognition of the tRNA and for the fidelity of protein synthesis. Publication Abstract from PubMed Human tRNA(His) guanylyltransferase (HsThg1) catalyzes the 3'-5' addition of guanosine triphosphate (GTP) to the 5'-end (-1 position) of tRNA(His), producing mature tRNA(His) In human cells, cytoplasmic and mitochondrial tRNA(His) has adenine (A) or cytidine (C), respectively, opposite to G-1 Little attention has been paid to the structural requirements of incoming GTP in 3'-5' nucleotidyl addition by HsThg1. In this study, we evaluated the incorporation efficiencies of various GTP analogs by HsThg1, and compared the reaction mechanism with that of Candida albicans Thg1 (CaThg1). HsThg1 incorporated GTP opposite A or C in the template most efficiently. In contrast to CaThg1, HsThg1 could incorporate UTP opposite A, and guanosine diphosphate (GDP) opposite C. These results suggest that HsThg1 could transfer not only GTP, but also other NTPs, by forming Watson-Crick (WC) hydrogen bonds between the incoming NTP and the template base. On the basis of the molecular mechanism, HsThg1 succeeded in labeling the 5'-end of tRNA(His) with biotinylated GTP. Structural analysis of HsThg1 was also performed in the presence of the mitochondrial tRNA(His) Structural comparison of HsThg1 with other Thg1 family enzymes suggested that the structural diversity of the C-terminal domain of the Thg1 enzymes might be involved in the formation of WC base pairing between the incoming GTP and template base. These findings provide new insights into an unidentified biological function of HsThg1 and also into the applicability of HsThg1 to the 5'-terminal modification of RNAs. Analysis of GTP addition in the reverse (3'-5') direction by human tRNA(His) guanylyltransferase.,Nakamura A, Wang D, Komatsu Y RNA. 2021 Mar 23. pii: rna.078287.120. doi: 10.1261/rna.078287.120. PMID:33758037 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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