Evidence map›Paper›PMID 37464011›Full record

ArticleCommunications chemistry2023

Roles of inter- and intramolecular tryptophan interactions in membrane-active proteins revealed by racemic protein crystallography.

Alexander J Lander, Laura Domínguez Mercado, Xuefei Li, Irshad Maajid Taily, Brandon L Findlay, Yi Jin, Louis Y P Luk

Abstract read
In one paragraph

Article in Communications chemistry, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
–field-weighted citation impact
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

9 citing papers in PubMed.

  1. Protein Structure Determination by Racemic and Quasi-Racemic X-Ray Crystallography.Chembiochem : a European journal of chemical biology · 2026
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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

7 authors.

Alexander J LanderSchool of Chemistry, Cardiff University, Main Building, Park Place, Cardiff, CF10 3AT, UK.ORCID http://orcid.org/0000-0003-0733-6597
Laura Domínguez MercadoDepartment of Chemistry & Biochemistry, Richard J. Renaud Science Complex, Concordia University, Montréal, Québec, H4B 1R6, Canada.
Xuefei LiSchool of Chemistry, Cardiff University, Main Building, Park Place, Cardiff, CF10 3AT, UK.
Irshad Maajid TailySchool of Chemistry, Cardiff University, Main Building, Park Place, Cardiff, CF10 3AT, UK.
Brandon L FindlayDepartment of Chemistry & Biochemistry, Richard J. Renaud Science Complex, Concordia University, Montréal, Québec, H4B 1R6, Canada. brandon.findlay@concordia.ca.ORCID http://orcid.org/0000-0001-7083-2513
Yi JinManchester Institute of Biotechnology, University of Manchester, Manchester, M1 7DN, UK. yi.jin@manchester.ac.uk.ORCID http://orcid.org/0000-0002-6927-4371
Louis Y P LukSchool of Chemistry, Cardiff University, Main Building, Park Place, Cardiff, CF10 3AT, UK. lukly@cardiff.ac.uk.ORCID http://orcid.org/0000-0002-7864-6261

Funding

Wellcome Trust
6 · The paper itself

Abstract

Tryptophan is frequently found on the surface of membrane-associated proteins that interact with the lipid membrane. However, because of their multifaceted interactions, it is difficult to pinpoint the structure-activity relationship of each tryptophan residue. Here, we describe the use of racemic protein crystallography to probe dedicated tryptophan interactions of a model tryptophan-rich bacteriocin aureocin A53 (AucA) by inclusion and/or exclusion of potential ligands. In the presence of tetrahedral anions that are isosteric to the head group of phospholipids, distinct tryptophan H-bond networks were revealed. H-bond donation by W40 was critical for antibacterial activity, as its substitution by 1-methyltryptophan resulted in substantial loss of activity against bacterial clinical isolates. Meanwhile, exclusion of tetrahedral ions revealed that W3 partakes in formation of a dimeric interface, thus suggesting that AucA is dimeric in solution and dissociated to interact with the phosphate head group in the presence of the lipid membrane. Based on these findings, we could predict the tryptophan residue responsible for activity as well as the oligomeric state of a distant homologue lacticin Q (48%).

Identifiers

PMID37464011
PMCPMC10354048

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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.