Evidence map›Paper›PMID 28291749›Full record

ArticleActa crystallographica. Section F, Structural biology communications2017

Proteolysis of truncated hemolysin A yields a stable dimerization interface.

Walter R P Novak, Basudeb Bhattacharyya, Daniel P Grilley, Todd M Weaver

Abstract read
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In one paragraph

Article in Acta crystallographica. Section F, Structural biology communications, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing 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

3 citing papers in PubMed.

  1. Progressive Backmapping of Highly Coarse-Grained Protein Models.bioRxiv : the preprint server for biology · 2026
    Article
  2. Article
  3. Bacterial pore-forming toxins.Microbiology (Reading, England) · 2022
    Article
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.

Walter R P NovakDepartment of Chemistry, Wabash College, 301 West Wabash Avenue, Crawfordsville, IN 47933, USA.
Basudeb BhattacharyyaDepartment of Chemistry and Biochemistry, University of Wisconsin-La Crosse, 1725 State Street, La Crosse, WI 54601, USA.
Daniel P GrilleyDepartment of Chemistry and Biochemistry, University of Wisconsin-La Crosse, 1725 State Street, La Crosse, WI 54601, USA.
Todd M WeaverDepartment of Chemistry and Biochemistry, University of Wisconsin-La Crosse, 1725 State Street, La Crosse, WI 54601, USA.

Funding

National Science Foundation, Division of Molecular and Cellular Biosciences MCB1050435
6 · The paper itself

Abstract

Wild-type and variant forms of HpmA265 (truncated hemolysin A) from Proteus mirabilis reveal a right-handed, parallel β-helix capped and flanked by segments of antiparallel β-strands. The low-salt crystal structures form a dimeric structure via the implementation of on-edge main-chain hydrogen bonds donated by residues 243-263 of adjacent monomers. Surprisingly, in the high-salt structures of two variants, Y134A and Q125A-Y134A, a new dimeric interface is formed via main-chain hydrogen bonds donated by residues 203-215 of adjacent monomers, and a previously unobserved tetramer is formed. In addition, an eight-stranded antiparallel β-sheet is formed from the flap regions of crystallographically related monomers in the high-salt structures. This new interface is possible owing to additional proteolysis of these variants after Tyr240. The interface formed in the high-salt crystal forms of hemolysin A variants may mimic the on-edge β-strand positioning used in template-assisted hemolytic activity.

Indexed as

Amino Acid SequenceBacterial ProteinsBinding SitesCloning, MolecularCrystallography, X-RayEscherichia coliGene ExpressionHemolysin ProteinsHydrogen BondingModels, MolecularMutationPlasmidsProtein BindingProtein Conformation, beta-StrandProtein Interaction Domains and MotifsProtein MultimerizationBacterial ProteinsHemolysin ProteinsRecombinant Proteinsalternate crystal formshemolysin AproteolysisProteus mirabilistwo-partner secretionβ-helix

Identifiers

PMID28291749
PMCPMC5349307

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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.