David G Waterman
Affiliation: University of York
- Crystal structure of Bacillus anthracis ThiI, a tRNA-modifying enzyme containing the predicted RNA-binding THUMP domainDavid G Waterman
York Structural Biology Laboratory, University of York, Chemistry Department, York YO10 5YW, UK
J Mol Biol 356:97-110. 2006..The inaccessibility of U8 in the canonical L-shaped form of tRNA, and the existence of a glycine-rich linker joining the catalytic and RNA-binding moieties of ThiI suggest that structural changes may occur in both molecules upon binding...
- Structure and activity of a novel archaeal β-CASP protein with N-terminal KH domainsAna P G Silva
York Structural Biology Laboratory, Department of Chemistry, University of York, York YO10 5YW, United Kingdom
Structure 19:622-32. 2011..We hypothesize that this nuclease degrades mRNAs of proteins targeted for degradation and so regulates archaeal RNA turnover, possibly in concert with the exosome...
- Structure of the Methanothermobacter thermautotrophicus exosome RNase PH ringC Leong Ng
York Structural Biology Laboratory, Chemistry Department, University of York, York YO10 5YW, England
Acta Crystallogr D Biol Crystallogr 66:522-8. 2010....
- Expression, purification, crystallization and preliminary X-ray studies of the TAN1 orthologue from Methanothermobacter thermautotrophicusAna P G Silva
York Structural Biology Laboratory, Department of Chemistry, University of York, York YO10 5YW, England
Acta Crystallogr Sect F Struct Biol Cryst Commun 64:1083-6. 2008..The molecule exists as a monomer in solution. X-ray data were collected to 2.85 A resolution from a native crystal belonging to space group P6(1)22 (or P6(5)22), with unit-cell parameters a = 69.9, c = 408.5 A...
- Conformational flexibility and molecular interactions of an archaeal homologue of the Shwachman-Bodian-Diamond syndrome proteinC Leong Ng
York Structural Biology Laboratory, Chemistry Department, University of York, York, YO10 5YW, UK
BMC Struct Biol 9:32. 2009..Although genomic and biophysical studies have suggested involvement of this protein in RNA metabolism and in ribosome biogenesis, its interacting partners remain largely unknown...
- S-Adenosyl-S-carboxymethyl-L-homocysteine: a novel cofactor found in the putative tRNA-modifying enzyme CmoARobert T Byrne
York Structural Biology Laboratory, Department of Chemistry, University of York, Heslington YO10 5DD, England
Acta Crystallogr D Biol Crystallogr 69:1090-8. 2013..Indeed, inspection of electron density for one such enzyme with known X-ray structure, PDB entry 1im8, suggests that the active site contains SCM-SAH and not SAM...