Titre :
  • Sequence-structure-function analysis of the bifunctional enzyme MnmC that catalyses the last two steps in the biosynthesis of hypermodified nucleoside mnm5s2U in tRNA.
Auteur : Roovers, Martine ; Oudjama, Yamina ; Kaminska, Katarzyna H ; Purta, Elzbieta ; Caillet, Joël ; Droogmans, Louis ; Bujnicki, Janusz Marek
Informations sur la publication : Proteins, 71, 4, (page 2076-2085)
Statut de publication : Publié, 2008-06
Sujet CREF : Sciences bio-médicales et agricoles
Mots-clés MeSH : Amino Acid Sequence
Amino Acid Substitution
Binding Sites
Catalysis
Computational Biology -- methods
Conserved Sequence
Escherichia coli Proteins -- analysis
Escherichia coli Proteins -- chemistry
Escherichia coli Proteins -- genetics
Escherichia coli Proteins -- metabolism
Flavin-Adenine Dinucleotide -- metabolism
Genetic Complementation Test
Ligands
Methylation
Models, Molecular
Molecular Sequence Data
Multienzyme Complexes -- analysis
Multienzyme Complexes -- chemistry
Multienzyme Complexes -- genetics
Multienzyme Complexes -- metabolism
Protein Binding
Protein Folding
Protein Structure, Secondary
Protein Structure, Tertiary
RNA, Bacterial -- biosynthesis
RNA, Transfer -- biosynthesis
Sequence Analysis
Sequence Deletion
Sequence Homology, Amino Acid
Static Electricity
Structure-Activity Relationship
Thiouridine -- analogs & derivatives
Thiouridine -- metabolism
Note : Journal Article
Research Support, Non-U.S. Gov't
SCOPUS: ar.j
FLWIN
Langue :
  • Anglais
Identificateurs : urn:issn:0887-3585 
info:doi/10.1002/prot.21918
info:pmid/18186482