Purification, crystallization and X-ray crystallographic studies of a Bacillus cereus MepR-like transcription factor, BC0657.

Min Uk Cho, Meong Il Kim, Minsun Hong

Abstract read

In one paragraph

Article in Acta crystallographica. Section F, Structural biology communications, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

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1citing papers in PubMed

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3 · Its place in the literature

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1 citing paper in PubMed.

Structure-based molecular characterization and regulatory mechanism of the LftR transcription factor from Listeria monocytogenes: Conformational flexibilities and a ligand-induced regulatory mechanism.PloS one · 2019
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5 · Who and what money

Authors and funding

3 authors.

Min Uk ChoDivision of Biological Science and Technology, Yonsei University, 1 Yonseidae-gil, Wonju-si, Ganwon-do 220-710, Republic of Korea.

Meong Il KimDivision of Biological Science and Technology, Yonsei University, 1 Yonseidae-gil, Wonju-si, Ganwon-do 220-710, Republic of Korea.

Minsun HongDivision of Biological Science and Technology, Yonsei University, 1 Yonseidae-gil, Wonju-si, Ganwon-do 220-710, Republic of Korea.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Transcription factors of the MarR family respond to internal and external changes and regulate a variety of biological functions through ligand association with microorganisms. MepR belongs to the MarR family, and its mutations are associated with the development of multidrug resistance in Staphylococcus aureus, which has caused a growing health problem. In this study, a Bacillus cereus MepR-like transcription regulator, BC0657, was crystallized. The BC0657 crystals diffracted to 2.05 Å resolution and belonged to either space group P6(2)22 or P6(4)22, with unit-cell parameters a = 110.57, b = 110.57, c = 67.29 Å. There was one molecule per asymmetric unit. Future comparative structural studies on BC0657 would extend knowledge of ligand-induced transcriptional regulatory mechanisms in the MarR family and would make a significant contribution to the design of antibiotic drugs against multidrug-resistant bacteria.

Indexed as

Amino Acid SequenceBacillus cereusBacterial ProteinsCrystallizationCrystallography, X-RayEscherichia coliGene ExpressionMolecular Sequence DataRecombinant ProteinsTranscription FactorsBacterial ProteinsRecombinant ProteinsTranscription FactorsBacillus cereusMepRtranscription factor

Identifiers

PMID26057803

DOI10.1107/S2053230X15007074

PMCPMC4461338

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.