Evidence map›Paper›PMID 34341189›Full record

ArticleActa crystallographica. Section F, Structural biology communications2021

LrpCBA pilus proteins of gut-dwelling Ligilactobacillus ruminis: crystallization and X-ray diffraction analysis.

Amar Prajapati, Airi Palva, Ingemar von Ossowski, Vengadesan Krishnan

Abstract read
In one paragraph

Article in Acta crystallographica. Section F, Structural biology communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

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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

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3 · Its place in the literature

Who cites it

1 citing paper in PubMed.

  1. Review
4 · The record

Corrections and comments

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5 · Who and what money

Authors and funding

4 authors.

Amar PrajapatiLaboratory of Structural Biology, Regional Centre for Biotechnology, NCR Biotech Science Cluster, Faridabad 121 001, India.
Airi PalvaDepartment of Veterinary Biosciences, University of Helsinki, Helsinki, Finland.
Ingemar von OssowskiDepartment of Veterinary Biosciences, University of Helsinki, Helsinki, Finland.
Vengadesan KrishnanLaboratory of Structural Biology, Regional Centre for Biotechnology, NCR Biotech Science Cluster, Faridabad 121 001, India.

Funding

Department of Biotechnology, Ministry of Science and Technology, India BT/PR22343/BRB/10/1570/2016Department of Biotechnology, Ministry of Science and Technology, India BT/PR5891/BRB/10/1098/2012
6 · The paper itself

Abstract

Adhesion to host surfaces for bacterial survival and colonization involves a variety of molecular mechanisms. Ligilactobacillus ruminis, a strict anaerobe and gut autochthonous (indigenous) commensal, relies on sortase-dependent pili (LrpCBA) for adherence to the intestinal inner walls, thereby withstanding luminal content flow. Here, the LrpCBA pilus is a promiscuous binder to gut collagen, fibronectin and epithelial cells. Structurally, the LrpCBA pilus displays a representative hetero-oligomeric arrangement and consists of three types of pilin subunit, each with its own location and function, i.e. tip LrpC for adhesion, basal LrpB for anchoring and backbone LrpA for length. To provide further structural insights into the assembly, anchoring and functional mechanisms of sortase-dependent pili, each of the L. ruminis pilus proteins was produced recombinantly for crystallization and X-ray diffraction analysis. Crystals of LrpC, LrpB, LrpA and truncated LrpA generated by limited proteolysis were obtained and diffracted to resolutions of 3.0, 1.5, 2.2 and 1.4 Å, respectively. Anomalous data were also collected from crystals of selenomethionine-substituted LrpC and an iodide derivative of truncated LrpA. Successful strategies for protein production, crystallization and derivatization are reported.

Indexed as

Amino Acid SequenceCrystallizationCrystallography, X-RayFimbriae, BacterialGastrointestinal MicrobiomeLactobacillusX-Ray Diffractionautochthonous commensalsbackbone LrpAbasal LrpBgut bacteriaintestineLigilactobacillus ruminisLrpCBA piluspilinstip LrpC

Identifiers

PMID34341189
PMCPMC8329715

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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.