Crystal structure of the N-terminal domain of the TyrR transcription factor responsible for gene regulation of aromatic amino acid biosynthesis and transport in Escherichia coli K12

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dc.contributor.authorVerger, Denis
dc.contributor.authorCarr, Paul D
dc.contributor.authorKwok, Terry
dc.contributor.authorOllis, David
dc.date.accessioned2015-12-07T22:43:11Z
dc.date.issued2007
dc.date.updated2015-12-07T11:16:14Z
dc.description.abstractThe X-ray structure of the N-terminal domain of TyrR has been solved to a resolution of 2.3 Å. It reveals a modular protein containing an ACT domain, a connecting helix, a PAS domain and a C-terminal helix. Two dimers are present in the asymmetric unit
dc.identifier.issn0022-2836
dc.identifier.urihttp://hdl.handle.net/1885/24893
dc.publisherElsevier
dc.sourceJournal of Molecular Biology
dc.subjectKeywords: aromatic amino acid; dimer; monomer; protein subunit; regulator protein; transcription factor; transcription factor TyrR; unclassified drug; amino acid synthesis; amino acid transport; amino terminal sequence; article; binding site; carboxy terminal seque activator; repressor; transcription regulation; TyrR protein; X-ray structure
dc.titleCrystal structure of the N-terminal domain of the TyrR transcription factor responsible for gene regulation of aromatic amino acid biosynthesis and transport in Escherichia coli K12
dc.typeJournal article
local.bibliographicCitation.issue1
local.bibliographicCitation.lastpage112
local.bibliographicCitation.startpage102
local.contributor.affiliationVerger, Denis, University of London
local.contributor.affiliationCarr, Paul D, College of Physical and Mathematical Sciences, ANU
local.contributor.affiliationKwok, Terry, University of Zurich
local.contributor.affiliationOllis, David, College of Physical and Mathematical Sciences, ANU
local.contributor.authoruidCarr, Paul D, u9206448
local.contributor.authoruidOllis, David, u9200080
local.description.embargo2037-12-31
local.description.notesImported from ARIES
local.identifier.absfor039999 - Chemical Sciences not elsewhere classified
local.identifier.ariespublicationu4005981xPUB35
local.identifier.citationvolume367
local.identifier.doi10.1016/j.jmb.2006.12.018
local.identifier.scopusID2-s2.0-33847084666
local.type.statusPublished Version

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