Structures of two bacterial resistance factors mediating tRNA-dependent aminoacylation of phosphatidylglycerol with lysine or alanine

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

Volumn 112, Issue 34, 2015, Pages 10691-10696

  Hebecker, Stefanie ^a   Krausze, Joern ^b   Hasenkampf, Tatjana ^a   Schneider, Julia ^a   Groenewold, Maike ^b   Reichelt, Joachim ^b   Jahn, Dieter ^a   Heinz, Dirk W ^b   Moser, Jürgen ^a  

^a TECHNICAL UNIVERSITY OF BRAUNSCHWEIG   (Germany)

^b HELMHOLTZ CENTRE FOR INFECTION RESEARCH   (Germany)

Author keywords

A PGS; L PGS; MprF; Structure; TRNA

Indexed keywords

ALANINE; AMINOACYL TRANSFER RNA; LYSINE; PHOSPHATIDYLGLYCEROL; ALANINE TRANSFER RNA; ALANYL-PHOSPHATIDYLGLYCEROL SYNTHASE, PSEUDOMONAS AERUGINOSA; AMINOACYLTRANSFERASE; BACTERIAL PROTEIN; HYBRID PROTEIN; LYSINE TRANSFER RNA; LYSYLPHOSPHATIDYLGLYCEROL;

AMINOACYLATION; ARTICLE; BACILLUS LICHENIFORMIS; CONTROLLED STUDY; ENZYME ACTIVE SITE; ENZYME STRUCTURE; ENZYME SUBSTRATE; MOLECULAR RECOGNITION; MUTAGENESIS; NONHUMAN; PRIORITY JOURNAL; PSEUDOMONAS AERUGINOSA; R FACTOR; RNA BINDING; X RAY CRYSTALLOGRAPHY; BACILLUS; BIOSYNTHESIS; CHEMICAL PHENOMENA; CHEMICAL STRUCTURE; CHEMISTRY; COMPARATIVE STUDY; CONFORMATION; ENZYME SPECIFICITY; ENZYMOLOGY; GENETICS; METABOLISM; MOLECULAR DOCKING; MOLECULAR GENETICS; NUCLEOTIDE SEQUENCE; PROTEIN CONFORMATION; SITE DIRECTED MUTAGENESIS; STRUCTURE ACTIVITY RELATION;

AMINOACYLATION; AMINOACYLTRANSFERASES; BACILLUS; BACTERIAL PROTEINS; BASE SEQUENCE; CATALYTIC DOMAIN; CRYSTALLOGRAPHY, X-RAY; HYDROPHOBIC AND HYDROPHILIC INTERACTIONS; LYSINE; MODELS, MOLECULAR; MOLECULAR DOCKING SIMULATION; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; NUCLEIC ACID CONFORMATION; PHOSPHATIDYLGLYCEROLS; PROTEIN CONFORMATION; PSEUDOMONAS AERUGINOSA; R FACTORS; RECOMBINANT FUSION PROTEINS; RNA, TRANSFER, ALA; RNA, TRANSFER, LYS; STRUCTURE-ACTIVITY RELATIONSHIP; SUBSTRATE SPECIFICITY;

EID: 84940478041     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1511167112     Document Type: Article

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