Evidence map›Paper›PMID 22437828›Full record

ArticleThe Journal of biological chemistry2012

Structural characterization of closely related O-antigen lipopolysaccharide (LPS) chain length regulators.

Sergei Kalynych, Deqiang Yao, James Magee, Miroslaw Cygler

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2012. 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
4.1field-weighted citation impact, top 6% 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, 31 citations in OpenAlex.

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  13. Quaternary structure of WzzB and WzzE polysaccharide copolymerases.Protein science : a publication of the Protein Society · 2015
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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

4 authors at 2 institutions in 1 country.

Sergei KalynychDepartment of Biochemistry, McGill University, Montreal, Quebec H3G 0B1, Canada.
Deqiang Yao
James Magee
Miroslaw Cygler
McGill University · CAUniversity of Saskatchewan · CA

Funding

Canadian Institutes of Health Research MOP-89787
6 · The paper itself

Abstract

The surface O-antigen polymers of gram-negative bacteria exhibit a modal length distribution that depends on dedicated chain length regulator periplasmic proteins (polysaccharide co-polymerases, PCPs) anchored in the inner membrane by two transmembrane helices. In an attempt to determine whether structural changes underlie the O-antigen modal length specification, we have determined the crystal structures of several closely related PCPs, namely two chimeric PCP-1 family members solved at 1.6 and 2.8 Å and a wild-type PCP-1 from Shigella flexneri solved at 2.8 Å. The chimeric proteins form circular octamers, whereas the wild-type WzzB from S. flexneri was found to be an open trimer. We also present the structure of a Wzz(FepE) mutant, which exhibits severe attenuation in its ability to produce very long O-antigen polymers. Our findings suggest that the differences in the modal length distribution depend primarily on the surface-exposed amino acids in specific regions rather than on the differences in the oligomeric state of the PCP protomers.

Indexed as

Amino Acid SequenceBacterial ProteinsCrystallography, X-RayEscherichia coliEscherichia coli ProteinsModels, MolecularMolecular Sequence DataO AntigensPeriplasmic ProteinsProtein MultimerizationProtein Structure, SecondaryProtein Structure, TertiarySequence Homology, Amino AcidShigella flexneriBacterial ProteinsEscherichia coli ProteinsO AntigensPeriplasmic ProteinswzzB protein, E coli

Identifiers

PMID22437828
PMCPMC3346132
OpenAlexW2043053060

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.