Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6611
pubmed:dateCreated
1997-1-23
pubmed:abstractText
Elongation factor G (EF-G) is a GTPase that is involved in the translocation of bacterial ribosomes along messenger RNA during protein biosynthesis. In contrast to current models, EF-G-dependent GTP hydrolysis is shown to precede, and greatly accelerate, the rearrangement of the ribosome that leads to translocation. Domain IV of the EF-G structure is crucial for both rapid translocation and subsequent release of the factor from the ribosome. By coupling the free energy of GTP hydrolysis to translocation, EF-G serves as a motor protein to drive the directional movement of transfer and messenger RNAs on the ribosome.
pubmed:commentsCorrections
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0028-0836
pubmed:author
pubmed:issnType
Print
pubmed:day
2
pubmed:volume
385
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
37-41
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:8985244-Binding Sites, pubmed-meshheading:8985244-Biological Transport, pubmed-meshheading:8985244-Biomechanics, pubmed-meshheading:8985244-Escherichia coli, pubmed-meshheading:8985244-GTP Phosphohydrolase-Linked Elongation Factors, pubmed-meshheading:8985244-Guanosine Diphosphate, pubmed-meshheading:8985244-Guanosine Triphosphate, pubmed-meshheading:8985244-Hydrolysis, pubmed-meshheading:8985244-Kinetics, pubmed-meshheading:8985244-Peptide Chain Elongation, Translational, pubmed-meshheading:8985244-Peptide Elongation Factor G, pubmed-meshheading:8985244-Peptide Elongation Factors, pubmed-meshheading:8985244-Protein Conformation, pubmed-meshheading:8985244-RNA, Transfer, pubmed-meshheading:8985244-Ribosomes, pubmed-meshheading:8985244-Sequence Deletion, pubmed-meshheading:8985244-Viomycin
pubmed:year
1997
pubmed:articleTitle
Hydrolysis of GTP by elongation factor G drives tRNA movement on the ribosome.
pubmed:affiliation
Institute of Molecular Biology, University of Witten/Herdecke, Germany.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't