Enzyme action at RNA-protein interface in DTD-like fold

The contemporary `RNA-protein world' is exemplified by close associations between many RNAs and proteins which are necessary to carry out important biological processes. DTD-like fold, which is involved in translational proofreading, represents such RNA-protein complexes (RNPCs). Interestingly,...

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Published inCurrent opinion in structural biology Vol. 53; pp. 107 - 114
Main Authors Routh, Satya Brata, Sankaranarayanan, Rajan
Format Journal Article
LanguageEnglish
Published England 01.12.2018
Subjects
Animals
Biocatalysis
Catalytic Domain
Cricetinae
Ribonucleases - metabolism
Ribosomes - metabolism
RNA, Transfer - metabolism
RNA, Transfer, Amino Acyl - metabolism
RNA-Binding Proteins - metabolism
Spliceosomes - metabolism
Substrate Specificity
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Summary:The contemporary `RNA-protein world' is exemplified by close associations between many RNAs and proteins which are necessary to carry out important biological processes. DTD-like fold, which is involved in translational proofreading, represents such RNA-protein complexes (RNPCs). Interestingly, it interacts with the substrates in the active site mostly through the main chain, and side chains are dispensable for both substrate specificity and catalysis. It functions at the RNA-protein interface to perform RNA-based catalysis using the 2'-OH of adenosine-76 of tRNA. Such catalytic RNPCs as the DTD-like fold also indicate the probable evolutionary trajectory for the transition from RNA-mediated catalysis to protein-based catalysis.
Bibliography:ObjectType-Article-2
SourceType-Scholarly Journals-1
ObjectType-Feature-3
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ObjectType-Review-1
ISSN:0959-440X
1879-033X
DOI:10.1016/j.sbi.2018.07.013