Evidence map›Paper›PMID 20010838›Full record

ArticleNature structural & molecular biology2010

Structure and mechanism of a pentameric formate channel.

Andrew B Waight, James Love, Da-Neng Wang

Open access · greenAbstract read
In one paragraph

Article in Nature structural & molecular biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.

0numbers the graph read from it
0cells of the map it votes in
53citing papers in PubMed
4.2field-weighted citation impact, top 5% 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

53 citing papers in PubMed, 99 citations in OpenAlex.

  1. Article
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  4. Review
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  6. Evolutionary Overview of Aquaporin Superfamily.Advances in experimental medicine and biology · 2023
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

3 authors at 2 institutions in 1 country.

Andrew B WaightThe Helen L. and Martin S. Kimmel Center for Biology and Medicine, Skirball Institute of Biomolecular Medicine, New York University School of Medicine, New York, New York, USA.
James Love
Da-Neng Wang
New York University · USNew York Structural Biology Center · US

Funding

Sub 9 at AECMU54GM075026 · NIGMS · NEW YORK STRUCTURAL BIOLOGY CENTER · PI WANG, DANENG · 2005 to 2009
$16.8M
Case Center for Synchrotron BiosciencesP30EB009998 · NIBIB · CASE WESTERN RESERVE UNIVERSITY · PI CHANCE, MARK R · 2009 to 2018
$8.4M
STRUCTURAL STUDIES OF SUGAR TRANSPORTERSR01DK053973 · NIDDK · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI WANG, DANENG · 1998 to 2014
$3.6M
Structural and Mechanistic Characterization of Neurotransmitter Reuptake InhibitiR01MH083840 · NIMH · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI WANG, DANENG · 2008 to 2012
$2.2M
Structural Basis of Tetracycline Resistance by Efflux Pump TetL.R01GM093825 · NIGMS · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI WANG, DANENG · 2010 to 2014
$1.4M
NIDDK NIH HHS R01 DK053973NIGMS NIH HHS R01 GM093825NIGMS NIH HHS U54 GM075026NIGMS NIH HHS U54GM075026NIMH NIH HHS R01 MH083840PHS HHS R01-073973
6 · The paper itself

Abstract

Formate transport across the inner membrane is a critical step in anaerobic bacterial respiration. Members of the formate/nitrite transport protein family function to shuttle substrate across the cytoplasmic membrane. In bacterial pathogens, the nitrite transport protein is involved in protecting bacteria from peroxynitrite released by host macrophages. We have determined the 2.13-A structure of the formate channel FocA from Vibrio cholerae, which reveals a pentamer in which each monomer possesses its own substrate translocation pore. Unexpectedly, the fold of the FocA monomer resembles that found in water and glycerol channels. The selectivity filter in FocA consists of a cytoplasmic slit and a central constriction ring. A 2.5-A high-formate structure shows two formate ions bound to the cytoplasmic slit via both hydrogen bonding and van der Waals interactions, providing a structural basis for the substrate selectivity of the channel.

Indexed as

Models, MolecularProtein ConformationProtein FoldingCrystallizationFormatesMembrane Transport ProteinsSubstrate SpecificityVibrio choleraeFormatesMembrane Transport Proteins

Identifiers

PMID20010838
PMCPMC3613427
OpenAlexW1999531492

What OpenQuestion holds

Textmetadata
LicenceTDM
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.