A conserved proline switch on the ribosome facilitates the recruitment and binding of trGTPases

Nature Structural and Molecular Biology

Volumn 19, Issue 4, 2012, Pages 403-410

  Wang, Li ^a,b   Yang, Fang ^a   Zhang, Dejiu ^a   Chen, Zhi ^a   Xu, Rui Ming ^a   Nierhaus, Knud H ^c   Gong, Weimin ^a,b   Qin, Yan ^a,b  

^a INSTITUTE OF BIOPHYSICS   (China)

^b UNIVERSITY OF SCIENCE AND TECHNOLOGY OF CHINA   (China)

^c MAX PLANCK INSTITUTE FOR MOLECULAR GENETICS   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

GUANOSINE TRIPHOSPHATASE; PEPTIDYLPROLYL ISOMERASE; PROLINE; PROLINE SWITCH 22; TRANSLATIONAL GUANOSINE TRIPHOSPHATASE; UNCLASSIFIED DRUG; ELONGATION FACTOR G; ESCHERICHIA COLI PROTEIN; GUANOSINE TRIPHOSPHATE;

ARTICLE; BACTERIAL CELL; CARBOXY TERMINAL SEQUENCE; CELL SURVIVAL; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME BINDING; ENZYME METABOLISM; ESCHERICHIA COLI; GENE MUTATION; ISOMERIZATION; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FUNCTION; PROTEIN SYNTHESIS; RIBOSOMAL FRAMESHIFTING; RIBOSOME; AMINO ACID SEQUENCE; CHEMICAL STRUCTURE; CHEMISTRY; ISOMERISM; METABOLISM; MOLECULAR GENETICS; SEQUENCE ALIGNMENT;

ESCHERICHIA COLI;

AMINO ACID SEQUENCE; CONSERVED SEQUENCE; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; GTP PHOSPHOHYDROLASES; GUANOSINE TRIPHOSPHATE; ISOMERISM; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PEPTIDE ELONGATION FACTOR G; PEPTIDYLPROLYL ISOMERASE; PROLINE; RIBOSOMES; SEQUENCE ALIGNMENT;

EID: 84861314628     PISSN: 15459993     EISSN: 15459985     Source Type: Journal    
DOI: 10.1038/nsmb.2254     Document Type: Article

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