Evidence map›Paper›PMID 26698633›Full record

ArticleThe Journal of biological chemistry2016

Structural Basis for Toughness and Flexibility in the C-terminal Passenger Domain of an Acinetobacter Trimeric Autotransporter Adhesin.

Kotaro Koiwai, Marcus D Hartmann, Dirk Linke, Andrei N Lupas, Katsutoshi Hori

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
2.4field-weighted citation impact, top 12% 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

27 citing papers in PubMed, 56 citations in OpenAlex.

  1. Article
  2. Designability of α-Helical Protein Filaments.Sub-cellular biochemistry · 2026
    Review
  3. Article
  4. Article
  5. Article
  6. Adhesion preference of the sticky bacteriumFrontiers in bioengineering and biotechnology · 2024
    Article
  7. Article
  8. Article
  9. Identification of the adhesive domain of AtaA fromFrontiers in bioengineering and biotechnology · 2022
    Article
  10. Article
  11. Review
  12. Mechanisms ProtectingInternational journal of molecular sciences · 2020
    Review
  13. Article
  14. Article
  15. TheVirulence · 2019
    Article
  16. Article
  17. Article
  18. Article
  19. Review
  20. The Mechanisms of Disease Caused byFrontiers in microbiology · 2019
    Review
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 3 institutions in 3 countries.

Kotaro KoiwaiFrom the Department of Biotechnology, Graduate School of Engineering, Nagoya University, Chikusa-ku, Nagoya 464-8603, Japan, the Structural Biology Research Center, Photon Factory, Institute of Materials Structure Science, High Energy Accelerator Research Organization, Tsukuba 305-0801, Japan.
Marcus D Hartmannthe Department of Protein Evolution, Max Planck Institute for Developmental Biology, 72076 Tübingen, Germany, and.
Dirk Linkethe Department of Protein Evolution, Max Planck Institute for Developmental Biology, 72076 Tübingen, Germany, and the Department of Biosciences, University of Oslo, 0316 Oslo, Norway.
Andrei N Lupasthe Department of Protein Evolution, Max Planck Institute for Developmental Biology, 72076 Tübingen, Germany, and.
Katsutoshi HoriFrom the Department of Biotechnology, Graduate School of Engineering, Nagoya University, Chikusa-ku, Nagoya 464-8603, Japan, khori@nubio.nagoya-u.ac.jp.
Max Planck Institute for Developmental Biology · DENagoya University · JPUniversity of Oslo · NO

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Trimeric autotransporter adhesins (TAAs) on the cell surface of Gram-negative pathogens mediate bacterial adhesion to host cells and extracellular matrix proteins. However, AtaA, a TAA in the nonpathogenic Acinetobacter sp. strain Tol 5, shows nonspecific high adhesiveness to abiotic material surfaces as well as to biotic surfaces. It consists of a passenger domain secreted by the C-terminal transmembrane anchor domain (TM), and the passenger domain contains an N-terminal head, N-terminal stalk, C-terminal head (Chead), and C-terminal stalk (Cstalk). The Chead-Cstalk-TM fragment, which is conserved in many Acinetobacter TAAs, has by itself the head-stalk-anchor architecture of a complete TAA. Here, we show the crystal structure of the Chead-Cstalk fragment, AtaA_C-terminal passenger domain (CPSD), providing the first view of several conserved TAA domains. The YadA-like head (Ylhead) of the fragment is capped by a unique structure (headCap), composed of three β-hairpins and a connector motif; it also contains a head insert motif (HIM1) before its last inner β-strand. The headCap, Ylhead, and HIM1 integrally form a stable Chead structure. Some of the major domains of the CPSD fragment are inherently flexible and provide bending sites for the fiber between segments whose toughness is ensured by topological chain exchange and hydrophobic core formation inside the trimer. Thus, although adherence assays using in-frame deletion mutants revealed that the characteristic adhesive sites of AtaA reside in its N-terminal part, the flexibility and toughness of the CPSD part provide the resilience that enables the adhesive properties of the full-length fiber across a wide range of conditions.

Indexed as

AcinetobacterAdhesins, BacterialCrystallography, X-RayProtein Structure, SecondaryProtein Structure, TertiaryType V Secretion SystemsAdhesins, BacterialType V Secretion SystemsAcinetobacteradhesinautotransporterbacterial adhesioncrystal structureGram-negative bacteriamembrane proteinprotein domainprotein structurestructure-function

Identifiers

PMID26698633
PMCPMC4759154
OpenAlexW2210192474

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.