The structure of NMB1585, a MarR-family regulator fromNeisseria meningitidis
Open Access
- 26 February 2009
- journal article
- structural communications
- Published by International Union of Crystallography (IUCr) in Acta Crystallographica Section F Structural Biology and Crystallization Communications
- Vol. 65 (3) , 204-209
- https://doi.org/10.1107/s174430910900414x
Abstract
The structure of the MarR-family transcription factor NMB1585 from Neisseria meningitidis has been solved using data extending to a resolution of 2.1 Å. Overall, the dimeric structure resembles those of other MarR proteins, with each subunit comprising a winged helix-turn-helix (wHtH) domain connected to an -helical dimerization domain. The spacing of the recognition helices of the wHtH domain indicates that NMB1585 is pre-configured for DNA binding, with a putative inducer pocket that is largely occluded by the side chains of two aromatic residues (Tyr29 and Trp53). NMB1585 was shown to bind to its own promoter region in a gel-shift assay, indicating that the protein acts as an auto-repressor.Keywords
This publication has 25 references indexed in Scilit:
- Structural Insight on the Mechanism of Regulation of the MarR Family of Proteins: High-Resolution Crystal Structure of a Transcriptional Repressor from Methanobacterium thermoautotrophicumJournal of Molecular Biology, 2008
- Crystal structure of the MarR family regulatory protein, ST1710, from Sulfolobus tokodaii strain 7Journal of Structural Biology, 2008
- Characterization of MobR, the 3-Hydroxybenzoate-responsive Transcriptional Regulator for the 3-Hydroxybenzoate Hydroxylase Gene of Comamonas testosteroni KH122-3sJournal of Molecular Biology, 2006
- Comparison of the RpoH-Dependent Regulon and General Stress Response in Neisseria gonorrhoeaeJournal of Bacteriology, 2006
- The Crystal Structure of the Transcriptional Regulator HucR from Deinococcus radiodurans Reveals a Repressor Preconfigured for DNA BindingJournal of Molecular Biology, 2006
- Crystal Structure of Enterococcus faecalis SlyA-like Transcriptional FactorPublished by Elsevier ,2003
- Crystallography & NMR System: A New Software Suite for Macromolecular Structure DeterminationActa Crystallographica Section D-Biological Crystallography, 1998
- The MarR Repressor of the Multiple Antibiotic Resistance (mar) Operon in Escherichia coli: Prototypic Member of a Family of Bacterial Regulatory Proteins Involved in Sensing Phenolic CompoundsMolecular Medicine, 1995
- Horizontal gene transfer of the Escherichia coli pap and prs pili operons as a mechanism for the development of tissue‐specific adhesive propertiesMolecular Microbiology, 1992
- Improved methods for building protein models in electron density maps and the location of errors in these modelsActa Crystallographica Section A Foundations of Crystallography, 1991