Structural basis for methyl-donor-dependent and sequence-specific binding to tRNA substrates by knotted methyltransferase TrmD

Proceedings of the National Academy of Sciences of the United States of America

Volumn 112, Issue 31, 2015, Pages E4197-E4205

  Ito, Takuhiro ^a,b   Masuda, Isao ^c   Yoshida, Ken Ichi ^a,b   Goto Ito, Sakurako ^a,b   Sekine, Shun Ichi ^a,b   Suh, Se Won ^d   Hou, Ya Ming ^c   Yokoyama, Shigeyuki ^a,b  

^a RIKEN   (Japan)

^b UNIVERSITY OF TOKYO   (Japan)

^c THOMAS JEFFERSON UNIVERSITY   (United States)

^d Seoul National University   (South Korea)

Author keywords

Rna modification; Spout methyltransferase; TrmD; X ray crystallography

Indexed keywords

BACTERIAL ENZYME; BACTERIAL RNA; GUANINE; METHIONINE; METHYLTRANSFERASE; S ADENOSYLMETHIONINE; SINEFUNGIN; TRANSFER RNA; TRANSFER RNA METHYLTRANSFERASE D; TREFOIL PEPTIDE; UNCLASSIFIED DRUG; ADENOSINE; ANTICODON; ESCHERICHIA COLI PROTEIN; TRANSFER RNA METHYLTRANSFERASE; TRMD PROTEIN, E COLI;

ANTICODON; ARTICLE; CARBOXY TERMINAL SEQUENCE; CRYSTAL STRUCTURE; ENZYME BINDING; HAEMOPHILUS INFLUENZAE; MOLECULAR RECOGNITION; MUTANT; NONHUMAN; PRIORITY JOURNAL; PROTEIN CONFORMATION; RNA BINDING; RNA METHYLATION; RNA SEQUENCE; THERMOTOGA MARITIMA; WILD TYPE; AMINO ACID SEQUENCE; ANALOGS AND DERIVATIVES; BINDING SITE; BIOCATALYSIS; CHEMICAL STRUCTURE; CHEMISTRY; ENZYME SPECIFICITY; ENZYMOLOGY; GENETICS; KINETICS; METABOLISM; METHYLATION; MOLECULAR GENETICS; NUCLEOTIDE SEQUENCE; SEQUENCE ALIGNMENT; STRUCTURE ACTIVITY RELATION; X RAY CRYSTALLOGRAPHY;

LOTUS;

ADENOSINE; AMINO ACID SEQUENCE; ANTICODON; BASE SEQUENCE; BINDING SITES; BIOCATALYSIS; CRYSTALLOGRAPHY, X-RAY; ESCHERICHIA COLI PROTEINS; GUANINE; HAEMOPHILUS INFLUENZAE; KINETICS; METHYLATION; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; RNA, TRANSFER; S-ADENOSYLMETHIONINE; SEQUENCE ALIGNMENT; STRUCTURE-ACTIVITY RELATIONSHIP; SUBSTRATE SPECIFICITY; THERMOTOGA MARITIMA; TRNA METHYLTRANSFERASES;

EID: 84938702956     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1422981112     Document Type: Article

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