Structure of the Escherichia coli Leucine-responsive Regulatory Protein Lrp Reveals a Novel Octameric Assembly
- 19 December 2006
- journal article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 366 (5), 1589-1602
- https://doi.org/10.1016/j.jmb.2006.12.032
Abstract
No abstract availableThis publication has 49 references indexed in Scilit:
- ilvIH Operon Expression in Escherichia coli Requires Lrp Binding to Two Distinct Regions of DNAJournal of Bacteriology, 2002
- Leucine-induced Dissociation of Escherichia coli Lrp Hexadecamers to OctamersJournal of Molecular Biology, 2002
- Modulation of Lrp action in Escherichia coli by leucine: effects on non-specific binding of Lrp to DNAJournal of Molecular Biology, 2001
- Leucine-regulated self-association of leucine-responsive regulatory protein (Lrp) from Escherichia coli 1 1Edited by M. F. MoodyJournal of Molecular Biology, 2001
- Electrostatics of nanosystems: Application to microtubules and the ribosomeProceedings of the National Academy of Sciences, 2001
- Crystal structure of the Lrp-like transcriptional regulator from the archaeon Pyrococcus furiosusThe EMBO Journal, 2001
- Structure of a binary complex of HhaI methyltransferase with S-adnosyl-l-methionine formed in the presence of a short non-specific DNA oligonucleotideJournal of Molecular Biology, 1999
- Conformational transitions and structural deformability of EcoRV endonuclease revealed by crystallographic analysisJournal of Molecular Biology, 1997
- The CCP4 suite: programs for protein crystallographyActa Crystallographica Section D-Biological Crystallography, 1994
- Interactive program for visualization and modelling of proteins, nucleic acids and small moleculesJournal of Molecular Graphics, 1986