Evidence map›Paper›PMID 25376905›Full record

ArticleBiochemistry2014

McbR/YncC: implications for the mechanism of ligand and DNA binding by a bacterial GntR transcriptional regulator involved in biofilm formation.

Dana M Lord, Ayse Uzgoren Baran, Valerie W C Soo, Thomas K Wood, Wolfgang Peti, Rebecca Page

Open access · greenAbstract read
In one paragraph

Article in Biochemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.4field-weighted citation impact, top 16% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

18 citing papers in PubMed, 41 citations in OpenAlex.

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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors at 1 institution in 1 country.

Dana M LordDepartment of Molecular Biology, Cell Biology and Biochemistry, ‡Graduate Program in Molecular Pharmacology and Physiology, and §Department of Molecular Pharmacology, Physiology and Biotechnology & Chemistry, Brown University , Providence, Rhode Island 02903, United States.
Ayse Uzgoren Baran
Valerie W C Soo
Thomas K Wood
Wolfgang Peti
Rebecca Page
Pennsylvania State University · US

Funding

UTERINE NK CELL HOMING FROM THE PERIPHERAL CIRCULATIONP20RR018728 · NCRR · WOMEN AND INFANTS HOSPITAL-RHODE ISLAND · PI BLISS, JOSEPH MARK · 2003 to 2011
$16.7M
Life Science and Biomedical technology Research center at NSLS-II LSBRP41GM111244 · NIGMS · BROOKHAVEN SCIENCE ASSOC-BROOKHAVEN LAB · PI MCSWEENEY, SEAN · 2014 to 2018
$16.4M
CENTER FOR CANCER SIGNALING NETWORKSP30RR031153 · NCRR · BROWN UNIVERSITY · PI ATWOOD, WALTER J · 2011 to 2011
$1.1M
Acquisition of an Orbitrap XL ETD Mass Spectrometer through Upgrading an LTQS10RR027027 · NCRR · BROWN UNIVERSITY · PI HAWROT, EDWARD · 2010 to 2010
$500k
CD SPECTROPHOTOMETER: STRUCTURAL BIOL, PROTEIN, MOLECULAR PHARMACOLOGYS10RR020923 · NCRR · BROWN UNIVERSITY · PI MIERKE, DALE F · 2006 to 2006
$105k
NCRR NIH HHS 1S10RR020923NCRR NIH HHS P20 RR018728NCRR NIH HHS P20RR018728NCRR NIH HHS P30 RR031153NCRR NIH HHS P30RR031153NCRR NIH HHS S10 RR020923NCRR NIH HHS S10 RR027027NCRR NIH HHS S10RR027027NCRR NIH HHS S10RR02763NIGMS NIH HHS P41 GM111244
6 · The paper itself

Abstract

MqsR-controlled colanic acid and biofilm regulator (McbR, also known as YncC) is the protein product of a highly induced gene in early Escherichia coli biofilm development and has been regarded as an attractive target for blocking biofilm formation. This protein acts as a repressor for genes involved in exopolysaccharide production and an activator for genes involved in stress response. To better understand the role of McbR in governing the switch from exponential growth to the biofilm state, we determined the crystal structure of McbR to 2.1 Å. The structure reveals McbR to be a member of the FadR C-terminal domain (FCD) family of the GntR superfamily of transcriptional regulators (this family was named after the first identified member, GntR, a transcriptional repressor of the gluconate operon of Bacillus subtilis). Previous to this study, only six of the predicted 2800 members of this family had been structurally characterized. Here, we identify the residues that constitute the McbR effector and DNA binding sites. In addition, comparison of McbR with other members of the FCD domain family shows that this family of proteins adopts highly distinct oligomerization interfaces, which has implications for DNA binding and regulation.

Indexed as

Amino Acid SequenceBinding SitesBiofilmsCrystallography, X-RayDNA, BacterialDNA-Binding ProteinsEscherichia coliEscherichia coli ProteinsGene Expression Regulation, BacterialModels, MolecularMolecular Sequence DataProtein BindingProtein ConformationProtein MultimerizationTranscription FactorsDNA, BacterialDNA-Binding ProteinsEscherichia coli ProteinsGntR protein, E coliMcbR protein, E coliTranscription Factors

Identifiers

PMID25376905
PMCPMC4245980
OpenAlexW2149218328

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.