Structural basis for the methylation of G1405 in 16s rRNA by aminoglycoside resistance methyltransferase Sgm from an antibiotic producer: A diversity of active sites in m7G methyltransferases

Nucleic Acids Research

Volumn 38, Issue 12, 2010, Pages 4120-4132

  Husain, Nilofer ^a   Tkaczuk, Karolina L ^b,c   Tulsidas, Shenoy Rajesh ^a   Kaminska, Katarzyna H ^b   Ĉubrilo, Sonja ^d   Maravić Vlahoviĉek, Gordana ^d   Bujnicki, Janusz M ^b,e   Sivaraman, J ^a  

^a NATIONAL UNIVERSITY OF SINGAPORE   (Singapore)

^b INTERNATIONAL INSTITUTE OF MOLECULAR AND CELL BIOLOGY   (Poland)

^c LODZ UNIVERSITY OF TECHNOLOGY   (Poland)

^d UNIVERSITY OF ZAGREB   (Croatia)

^e ADAM MICKIEWICZ UNIVERSITY   (Poland)

Author keywords

[No Author keywords available]

Indexed keywords

AMINOGLYCOSIDE; M7G METHYLTRANSFERASE; METHYLTRANSFERASE; RIBOSOME RNA; RNA 16S; S ADENOSYLHOMOCYSTEINE; S ADENOSYLMETHIONINE; SISOMICIN GENTAMICIN METHYLTRANSFERASE; UNCLASSIFIED DRUG; 16S RRNA - M7G METHYLTRANSFERASE; 16S RRNA M7G METHYLTRANSFERASE; ANTIINFECTIVE AGENT; BACTERIAL PROTEIN;

ARTICLE; CONTROLLED STUDY; ENZYME ACTIVE SITE; ENZYME BINDING; ENZYME INHIBITION; ENZYME SPECIFICITY; ENZYME STRUCTURE; ISOTHERMAL TITRATION CALORIMETRY; METHYLATION; MUTAGENESIS; NONHUMAN; PRIORITY JOURNAL; PROTEIN FOOTPRINTING; PROTEIN RNA BINDING; AMINO ACID SEQUENCE; ANTIBIOTIC RESISTANCE; BIOSYNTHESIS; CALORIMETRY; CHEMICAL STRUCTURE; CHEMISTRY; ENZYMOLOGY; METABOLISM; MICROMONOSPORA; MOLECULAR GENETICS; NUCLEOTIDE SEQUENCE; SEQUENCE HOMOLOGY; SMALL RIBOSOMAL SUBUNIT;

BACTERIA (MICROORGANISMS); MICROMONOSPORA ZIONENSIS;

AMINO ACID SEQUENCE; AMINOGLYCOSIDES; ANTI-BACTERIAL AGENTS; BACTERIAL PROTEINS; BASE SEQUENCE; CALORIMETRY; CATALYTIC DOMAIN; CONSERVED SEQUENCE; DRUG RESISTANCE, BACTERIAL; METHYLATION; METHYLTRANSFERASES; MICROMONOSPORA; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; RIBOSOME SUBUNITS, SMALL, BACTERIAL; RNA, RIBOSOMAL, 16S; S-ADENOSYLHOMOCYSTEINE; S-ADENOSYLMETHIONINE; SEQUENCE HOMOLOGY, AMINO ACID;

EID: 77955084302     PISSN: 03051048     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gkq122     Document Type: Article

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