Linked Life Data

17374541

Source:http://linkedlifedata.com/resource/pubmed/id/17374541

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2007-4-9
pubmed:databankReference
pubmed:abstractText
A 16-residue peptide, called Tip, induces the tetracycline repressor TetR as efficiently as the antibiotic tetracycline when fused to the N or C terminus of another protein. This is unusual because the majority of in vitro selected peptides, such as Tip, inhibit protein function, and agonist peptides are only rarely identified. We elucidated the atomic mechanism of TetR induction by Tip from crystal structures of TetR in complex with Tip and of free TetR. Peptide induction ultimately results in the same movements of DNA reading heads, but Tip accomplishes this by very different molecular interactions from tetracycline involving important contacts to the TetR surface. As a direct consequence, an alternate pathway of allostery becomes possible that makes ample use of intersubunit interactions. For the first time it is possible to show in atomic detail how a small molecule controlled bacterial transcription factor such as TetR becomes responsive to protein-protein interactions, characteristic of gene transcription regulation in higher organisms.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0022-2836
pubmed:author
pubmed:issnType
Print
pubmed:day
4
pubmed:volume
368
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
780-90
pubmed:meshHeading
pubmed:year
2007
pubmed:articleTitle
How an agonist peptide mimics the antibiotic tetracycline to induce Tet-repressor.
pubmed:affiliation
Lehrstuhl für Biotechnik, Institut für Biologie, Friedrich-Alexander-Universität Erlangen-Nürnberg, Erlangen, Germany.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't