Evidence map›Paper›PMID 28683919›Full record

ReviewAdvances in protein chemistry and structural biology2017

Sortase Transpeptidases: Structural Biology and Catalytic Mechanism.

Alex W Jacobitz, Michele D Kattke, Jeff Wereszczynski, Robert T Clubb

Open access · greenAbstract readReview
In one paragraph

Review in Advances in protein chemistry and structural biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 66 papers.

0numbers the graph read from it
0cells of the map it votes in
66citing papers in PubMed
20.8field-weighted citation impact, top 1% 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

66 citing papers in PubMed, 146 citations in OpenAlex.

  1. Article
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  6. Amino acid variants at the P94 position inbioRxiv : the preprint server for biology · 2026
    Article
  7. Article
  8. A Putative Interaction between the Transmembrane Domains ofThe journal of physical chemistry. B · 2025
    Article
  9. Article
  10. Article
  11. The Exoproteome and Surfaceome of ToxigenicJournal of proteome research · 2025
    Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Review
  20. Article

6 more citing papers are in PubMed but not listed here.

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.

Alex W JacobitzThe Molecular Biology Institute and the UCLA-DOE Institute of Genomics and Proteomics, University of California, Los Angeles, CA, United States.
Michele D KattkeThe Molecular Biology Institute and the UCLA-DOE Institute of Genomics and Proteomics, University of California, Los Angeles, CA, United States.
Jeff WereszczynskiCenter for Molecular Study of Condensed Soft Matter, Illinois Institute of Technology, Chicago, IL, United States.
Robert T ClubbThe Molecular Biology Institute and the UCLA-DOE Institute of Genomics and Proteomics, University of California, Los Angeles, CA, United States. Electronic address: rclubb@mbi.ucla.edu.
University of California, Los Angeles · USIllinois Institute of Technology · US

Funding

Cell Surface Protein Anchoring in Gram-Positive BacteriaR01AI052217 · NIAID · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI Robert Thompson Clubb · 2002 to 2026
$8.5M
NIAID NIH HHS R01 AI052217
6 · The paper itself

Abstract

Gram-positive bacteria use sortase cysteine transpeptidase enzymes to covalently attach proteins to their cell wall and to assemble pili. In pathogenic bacteria sortases are potential drug targets, as many of the proteins that they display on the microbial surface play key roles in the infection process. Moreover, the Staphylococcus aureus Sortase A (SaSrtA) enzyme has been developed into a valuable biochemical reagent because of its ability to ligate biomolecules together in vitro via a covalent peptide bond. Here we review what is known about the structures and catalytic mechanism of sortase enzymes. Based on their primary sequences, most sortase homologs can be classified into six distinct subfamilies, called class A-F enzymes. Atomic structures reveal unique, class-specific variations that support alternate substrate specificities, while structures of sortase enzymes bound to sorting signal mimics shed light onto the molecular basis of substrate recognition. The results of computational studies are reviewed that provide insight into how key reaction intermediates are stabilized during catalysis, as well as the mechanism and dynamics of substrate recognition. Lastly, the reported in vitro activities of sortases are compared, revealing that the transpeptidation activity of SaSrtA is at least 20-fold faster than other sortases that have thus far been characterized. Together, the results of the structural, computational, and biochemical studies discussed in this review begin to reveal how sortases decorate the microbial surface with proteins and pili, and may facilitate ongoing efforts to discover therapeutically useful small molecule inhibitors.

Indexed as

AminoacyltransferasesBacterial ProteinsCatalytic DomainCysteine EndopeptidasesGram-Positive BacteriaGram-Positive Bacterial InfectionsHumansModels, MolecularProtein ConformationStaphylococcal InfectionsStaphylococcus aureusSubstrate SpecificityAminoacyltransferasesBacterial ProteinsCysteine Endopeptidasessortase AMechanismSortaseStructureTranspeptidase

Identifiers

PMID28683919
PMCPMC5718342
OpenAlexW2621794112

What OpenQuestion holds

Textmetadata
LicenceTDM
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.