The polynucleotide ligase and RNA capping enzyme superfamily of covalent nucleotidyltransferases Journal Article
| Authors: | Shuman, S.; Lima, C. D. |
| Article Title: | The polynucleotide ligase and RNA capping enzyme superfamily of covalent nucleotidyltransferases |
| Abstract: | ATP- and NAD +-dependent DNA ligases, ATP-dependent RNA ligases and GTP-dependent mRNA capping enzymes comprise a superfamily of proteins that catalyze nucleotidyl transfer to polynucleotide 5′ ends via covalent enzyme-(lysyl-N)-NMP intermediates. The superfamily is defined by five peptide motifs that line the nucleotide-binding pocket and contribute amino acid sidechains essential for catalysis. Early crystal structures revealed a shared core tertiary structure for DNA ligases and capping enzymes, which are composed minimally of a nucleotidyltransferase domain fused to a distal OB-fold domain. Recent structures of viral and bacterial DNA ligases, and a fungal mRNA capping enzyme underscore how the substrate-binding and chemical steps of the ligation and capping pathways are coordinated with large rearrangements of the component protein domains and with remodeling of the atomic contacts between the enzyme and the nucleotide at the active site. The first crystal structure of an RNA ligase suggests that contemporary DNA ligases, RNA ligases and RNA capping enzymes evolved by fusion of ancillary effector domains to an ancestral catalytic module involved in RNA repair. © 2004 Elsevier Ltd. All rights reserved. |
| Keywords: | protein expression; review; nonhuman; drug targeting; protein conformation; protein domain; models, biological; protein binding; evolution; enzyme activation; structure-activity relationship; bacteria (microorganisms); amino acid sequence; enzyme analysis; rna caps; nucleotide sequence; substrate specificity; binding site; models, molecular; binding sites; protein structure; polydeoxyribonucleotide synthase; enzyme specificity; virus; dynamics; models, chemical; fungus; bacterium; enzyme mechanism; amino acid motifs; cap binding protein; nucleotidyltransferase; nucleotidyltransferases; polynucleotide ligases; priority journal |
| Journal Title: | Current Opinion in Structural Biology |
| Volume: | 14 |
| Issue: | 6 |
| ISSN: | 0959-440X |
| Publisher: | Elsevier Inc. |
| Date Published: | 2004-12-01 |
| Start Page: | 757 |
| End Page: | 764 |
| Language: | English |
| DOI: | 10.1016/j.sbi.2004.10.006 |
| PROVIDER: | scopus |
| PUBMED: | 15582400 |
| DOI/URL: | |
| Notes: | Curr. Opin. Struct. Biol. -- Cited By (since 1996):107 -- Export Date: 16 June 2014 -- CODEN: COSBE -- Source: Scopus |
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