CCA-addition in the cold: Structural characterization of the psychrophilic CCA-adding enzyme from the permafrost bacterium Planococcus halocryophilus
Open Access
- 21 October 2021
- journal article
- research article
- Published by American Association for the Advancement of Science (AAAS) in Computational and Structural Biotechnology Journal
- Vol. 19, 5845-5855
Abstract
• A high-resolution structure of a psychrophilic RNA polymerase contributes to our knowledge of cold adaptation. • While catalytic core motifs are conserved, at least one shows cold adaptation. • Loss of helix-capping increases structural flexibility in a catalytic core motif. • Overall reduction of alpha-helical elements appears as a strategy for cold adaptation.Keywords
This publication has 61 references indexed in Scilit:
- CAPS-DB: a structural classification of helix-capping motifsNucleic Acids Research, 2011
- Unusual evolution of a catalytic core element in CCA-adding enzymesNucleic Acids Research, 2010
- Mechanism for the definition of elongation and termination by the class II CCA‐adding enzymeThe EMBO Journal, 2009
- Evolution of tRNA nucleotidyltransferases: A small deletion generated CC-adding enzymesProceedings of the National Academy of Sciences, 2008
- A comparative analysis of CCA-adding enzymes from human and E. coli: Differences in CCA addition and tRNA 3′-end repairBiochimie, 2008
- Phasercrystallographic softwareJournal of Applied Crystallography, 2007
- Reengineering CCA-adding enzymes to function as (U,G)- or dCdCdA-adding enzymes or poly(C,A) and poly(U,G) polymerasesProceedings of the National Academy of Sciences, 2007
- Psychrophilic microorganisms: challenges for lifeEMBO Reports, 2006
- Coot: model-building tools for molecular graphicsActa Crystallographica Section D Structural Biology, 2004
- CRYSOL– a Program to Evaluate X-ray Solution Scattering of Biological Macromolecules from Atomic CoordinatesJournal of Applied Crystallography, 1995