Structure of yeast phenylalanine transfer RNA at 2.5 A resolution.
AUTOR(ES)
Ladner, J E
RESUMO
The x-ray analysis of the monoclinic form of yeast tRNAPhe has been taken to a resolution of 2.5 A by the method of isomorphous replacement. The model proposed at 3 A has been confirmed and extended to reveal additional features of the tertiary structure and of the stereochemistry. An extensive hydrogen bonding network is described involving specific interactions between bases and the ribose-phosphate backbone. The structure of a G-U base pair has been solved.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=388732Documentos Relacionados
- Structure and heme environment of beef liver catalase at 2.5 A resolution.
- Three-dimensional structure of bovine pancreatic DNase I at 2.5 A resolution.
- Crystal structure of recombinant human T-cell cyclophilin A at 2.5 A resolution.
- Three-dimensional structure of transketolase, a thiamine diphosphate dependent enzyme, at 2.5 A resolution.
- The Three-Dimensional Structure of Yeast Phenylalanine Transfer RNA: Shape of the Molecule at 5.5-Å Resolution