Evidence map›Paper›PMID 25945572›Full record

ArticleActa crystallographica. Section D, Biological crystallography2015

Structures of Bacteroides fragilis uridine 5'-diphosphate-N-acetylglucosamine (UDP-GlcNAc) acyltransferase (BfLpxA).

Alice Ngo, Kai T Fong, Daniel L Cox, Xi Chen, Andrew J Fisher

Open access · bronzeAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Acta crystallographica. Section D, Biological crystallography, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.2field-weighted citation impact, top 44% 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

4 citing papers in PubMed, 5 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

5 authors at 1 institution in 1 country.

Alice NgoDepartment of Chemistry, University of California, One Shields Avenue, Davis, CA 95616, USA.
Kai T FongDepartment of Chemistry, University of California, One Shields Avenue, Davis, CA 95616, USA.
Daniel L CoxDepartment of Physics, University of California, One Shields Avenue, Davis, CA 95616, USA.
Xi ChenDepartment of Chemistry, University of California, One Shields Avenue, Davis, CA 95616, USA.
Andrew J FisherDepartment of Chemistry, University of California, One Shields Avenue, Davis, CA 95616, USA.
University of California, Davis · US

Funding

ZWITTERION SURFACTANT DDMAB FOR IMPROV STABIL OF PROTEINP41RR001209 · NCRR · STANFORD UNIVERSITY · PI GONZALEZ, ANA M · 1985 to 2011
$38.9M
X-ray Absorption Spectroscopy (XAS) pp.711-759P41GM103393 · NIGMS · STANFORD UNIVERSITY · PI HODGSON, KEITH O · 2012 to 2019
$30.6M
Oligosaccharides as antimicrobials and prebioticsR01HD065122 · NICHD · UNIVERSITY OF CALIFORNIA AT DAVIS · PI CHEN, XI · 2010 to 2013
$1.8M
New chemoenzymatic methods for synthesizing complex carbohydratesR01GM094523 · NIGMS · UNIVERSITY OF CALIFORNIA AT DAVIS · PI CHEN, XI · 2013 to 2016
$1.2M
NCRR NIH HHS P41 RR001209NCRR NIH HHS P41RR001209NICHD NIH HHS R01 HD065122NICHD NIH HHS R01HD065122NIGMS NIH HHS P41 GM103393NIGMS NIH HHS P41GM103393NIGMS NIH HHS R01 GM094523NIGMS NIH HHS R01GM094523
6 · The paper itself

Abstract

Uridine 5'-diphosphate-N-acetylglucosamine (UDP-GlcNAc) acyltransferase (LpxA) catalyzes a reversible reaction for adding an O-acyl group to the GlcNAc in UDP-GlcNAc in the first step of lipid A biosynthesis. Lipid A constitutes a major component of lipopolysaccharides, also referred to as endotoxins, which form the outer monolayer of the outer membrane of Gram-negative bacteria. Ligand-free and UDP-GlcNAc-bound crystal structures of LpxA from Bacteroides fragilis NCTC 9343, the most common pathogenic bacteria found in abdominal abscesses, have been determined and are presented here. The enzyme crystallizes in a cubic space group, with the crystallographic threefold axis generating the biological functional homotrimer and with each monomer forming a nine-rung left-handed β-helical (LβH) fold in the N-terminus followed by an α-helical motif in the C-terminus. The structure is highly similar to LpxA from other organisms. Yet, despite sharing a similar LβH structure with LpxAs from Escherichia coli and others, previously unseen calcium ions are observed on the threefold axis in B. fragilis LpxA to help stabilize the trimeric assembly.

Indexed as

AcyltransferasesAmino Acid SequenceBacteroides fragilisCrystallography, X-RayModels, MolecularMolecular Sequence DataMolecular StructureProtein ConformationSequence Homology, Amino AcidUridine Diphosphate N-Acetylglucosamineacyl-(acyl-carrier-protein)-UDP-N-acetylglucosamine acyltransferaseAcyltransferasesUridine Diphosphate N-Acetylglucosamineleft-handed β-helixlipid ALpxAUDP-N-acetylglucosamine acyltransferase

Identifiers

PMID25945572
PMCPMC4427197
OpenAlexW2045017092

What OpenQuestion holds

Textmetadata
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Registered trials

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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.