Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
2001-3-20
pubmed:databankReference
pubmed:abstractText
The LrpA protein from the hyperthermophilic archaeon Pyrococcus furiosus belongs to the Lrp/AsnC family of transcriptional regulatory proteins, of which the Escherichia coli leucine-responsive regulatory protein is the archetype. Its crystal structure has been determined at 2.9 A resolution and is the first for a member of the Lrp/AsnC family, as well as one of the first for a transcriptional regulator from a hyperthermophile. The structure consists of an N-terminal domain containing a helix-turn-helix (HtH) DNA-binding motif, and a C-terminal domain of mixed alpha/beta character reminiscent of a number of RNA- and DNA-binding domains. Pyrococcus furiosus LrpA forms a homodimer mainly through interactions between the antiparallel beta-sheets of the C-terminal domain, and further interactions lead to octamer formation. The LrpA structure suggests how the protein might bind and possibly distort its DNA substrate through use of its HtH motifs and control gene expression. A possible location for an effector binding site is proposed by using sequence comparisons with other members of the family coupled to mutational analysis.
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/11230123-10097083, http://linkedlifedata.com/resource/pubmed/commentcorrection/11230123-10973967, http://linkedlifedata.com/resource/pubmed/commentcorrection/11230123-1328886, http://linkedlifedata.com/resource/pubmed/commentcorrection/11230123-15299374, http://linkedlifedata.com/resource/pubmed/commentcorrection/11230123-15299926, http://linkedlifedata.com/resource/pubmed/commentcorrection/11230123-1758883, http://linkedlifedata.com/resource/pubmed/commentcorrection/11230123-2025413, http://linkedlifedata.com/resource/pubmed/commentcorrection/11230123-2040596, http://linkedlifedata.com/resource/pubmed/commentcorrection/11230123-2115869, http://linkedlifedata.com/resource/pubmed/commentcorrection/11230123-2864330, http://linkedlifedata.com/resource/pubmed/commentcorrection/11230123-3903514, http://linkedlifedata.com/resource/pubmed/commentcorrection/11230123-3909107, http://linkedlifedata.com/resource/pubmed/commentcorrection/11230123-5551392, http://linkedlifedata.com/resource/pubmed/commentcorrection/11230123-6261152, http://linkedlifedata.com/resource/pubmed/commentcorrection/11230123-7585249, http://linkedlifedata.com/resource/pubmed/commentcorrection/11230123-7665463, http://linkedlifedata.com/resource/pubmed/commentcorrection/11230123-7792597, http://linkedlifedata.com/resource/pubmed/commentcorrection/11230123-7835344, http://linkedlifedata.com/resource/pubmed/commentcorrection/11230123-7968922, http://linkedlifedata.com/resource/pubmed/commentcorrection/11230123-7984237, http://linkedlifedata.com/resource/pubmed/commentcorrection/11230123-8137808, http://linkedlifedata.com/resource/pubmed/commentcorrection/11230123-8144448, http://linkedlifedata.com/resource/pubmed/commentcorrection/11230123-8381875, http://linkedlifedata.com/resource/pubmed/commentcorrection/11230123-8429549, http://linkedlifedata.com/resource/pubmed/commentcorrection/11230123-8432705, http://linkedlifedata.com/resource/pubmed/commentcorrection/11230123-8433969, http://linkedlifedata.com/resource/pubmed/commentcorrection/11230123-8561478, http://linkedlifedata.com/resource/pubmed/commentcorrection/11230123-875032, http://linkedlifedata.com/resource/pubmed/commentcorrection/11230123-9675798, http://linkedlifedata.com/resource/pubmed/commentcorrection/11230123-9716374, http://linkedlifedata.com/resource/pubmed/commentcorrection/11230123-9852962
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0261-4189
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
20
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
990-7
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed-meshheading:11230123-Amino Acid Sequence, pubmed-meshheading:11230123-Archaeal Proteins, pubmed-meshheading:11230123-Binding Sites, pubmed-meshheading:11230123-Calorimetry, Differential Scanning, pubmed-meshheading:11230123-Crystallography, X-Ray, pubmed-meshheading:11230123-DNA, pubmed-meshheading:11230123-DNA-Binding Proteins, pubmed-meshheading:11230123-Dimerization, pubmed-meshheading:11230123-Escherichia coli Proteins, pubmed-meshheading:11230123-Gene Expression Regulation, Archaeal, pubmed-meshheading:11230123-Leucine, pubmed-meshheading:11230123-Leucine-Responsive Regulatory Protein, pubmed-meshheading:11230123-Models, Molecular, pubmed-meshheading:11230123-Molecular Sequence Data, pubmed-meshheading:11230123-Mutation, pubmed-meshheading:11230123-Nucleic Acid Conformation, pubmed-meshheading:11230123-Protein Binding, pubmed-meshheading:11230123-Protein Structure, Secondary, pubmed-meshheading:11230123-Protein Structure, Tertiary, pubmed-meshheading:11230123-Pyrococcus furiosus, pubmed-meshheading:11230123-Sequence Alignment, pubmed-meshheading:11230123-Transcription Factors
pubmed:year
2001
pubmed:articleTitle
Crystal structure of the Lrp-like transcriptional regulator from the archaeon Pyrococcus furiosus.
pubmed:affiliation
Krebs Institute for Biomolecular Research, Department of Molecular Biology and Biotechnology, University of Sheffield, Western Bank, Sheffield S10 2TN, UK.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't