Linked Life Data

9738479

Source:http://linkedlifedata.com/resource/pubmed/id/9738479

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1-2
pubmed:dateCreated
1998-9-29
pubmed:abstractText
Three variants of Thermus thermophilus EF-G with mutations in the loop at the distal end of its domain IV were obtained. The replacement of His-573 by Ala and double mutation H573A/D576A did not influence the functional activity of EF-G. On the other hand, the insertion of six amino acids into the loop between residues Asp-576 and Ser-577 reduced the translocational activity of EF-G markedly, while its GTPase activity was not affected. It is concluded that the native conformation of the loop is important for the factor-promoted translocation in the ribosome. The functional importance of the entire EF-G domain IV is discussed.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0014-5793
pubmed:author
pubmed:issnType
Print
pubmed:day
28
pubmed:volume
434
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
205-8
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1998
pubmed:articleTitle
An intact conformation at the tip of elongation factor G domain IV is functionally important.
pubmed:affiliation
Institute of Protein Research, Russian Academy of Sciences, Pushchino, Moscow Region.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't