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PMID: 10943889 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

The crystal structure of yeast phenylalanine tRNA at 1.93 A resolution: a classic structure revisited.

RNA (New York, N.Y.) ·Vol. 6 ·No. 8 ·2000-08-00 ·Pages 1091-105

Shi H, Moore PB

Abstract

The crystal structure of the monoclinic form of yeast phenylalanine tRNA has been redetermined at a resolution of 1.93 A. The structure of yeast tRNAphe described here is more accurate than its predecessors not only because it incorporates higher resolution data, but also because it has been refined using techniques that had not been developed when its predecessors were determined more than 20 years ago. The 1.93 A resolution version of this structure differs interestingly from its predecessors in its details. In loop regions particularly, the backbone torsion angles in the new structure are not the same as those reported earlier. Several new divalent cation binding sites have been identified, and the water structure that has emerged is also different.

MeSH Terms
Base Sequence Binding Sites Cations Cobalt/metabolism Crystallography, X-Ray Magnesium/metabolism Manganese/metabolism Models, Molecular Molecular Sequence Data Nucleic Acid Conformation RNA, Fungal/metabolism RNA, Transfer, Phe/chemistry,ultrastructure Saccharomyces cerevisiae/genetics,ultrastructure Torsion Abnormality Water/metabolism
Chemicals
Cations RNA, Fungal RNA, Transfer, Phe Water Cobalt Manganese Magnesium
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Shi H
Department of Chemistry, Yale University, New Haven, Connecticut 06520-8107, USA.
Moore P B
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23 references, click to expand
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Article Info
Journal
RNA (New York, N.Y.)
Abbr.
RNA
ISSN
1355-8382
DOI
10.1017/s1355838200000364
Published
2000-08-00
Pages
1091-105
Language
English
Region
United States
NLM ID
9509184
PMCID
PMC1369984
Subset
IM
Grants
NIGMS NIH HHS · GM 54216 · United States
External Links
PubMed source DOI: 10.1017/s1355838200000364 PMC Full Text View journal details
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