ArticleThe Journal of biological chemistry2010
The Sortase A enzyme that attaches proteins to the cell wall of Bacillus anthracis contains an unusual active site architecture.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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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.
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Who cites it
30 citing papers in PubMed, 62 citations in OpenAlex.
- Amino Acid Variants at the P94 Position inBiochemistry · 2026Article
- Amino acid variants at the P94 position inbioRxiv : the preprint server for biology · 2026Article
- Exploring Plant-Based Compounds as Alternatives for TargetingInternational journal of molecular sciences · 2024Article
- Structural and functional insights of sortases and their interactions with antivirulence compounds.Current research in structural biology · 2024Review
- Challenges in the use of sortase and other peptide ligases for site-specific protein modification.Chemical Society reviews · 2022Review
- The Fusaric Acid Derivative qy17 InhibitsFrontiers in microbiology · 2022Article
- The divergent roles of sortase in the biology of Gram-positive bacteria.Cell surface (Amsterdam, Netherlands) · 2021Review
- Interrogation ofSaudi journal of biological sciences · 2021Article
- Genetics, Structure, and Function of Group A Streptococcal Pili.Frontiers in microbiology · 2021Review
- TheMicroorganisms · 2020Review
- Article
- Kinetics and Optimization of the Lysine-Isopeptide Bond Forming Sortase Enzyme fromBioconjugate chemistry · 2020Article
- A comprehensive in silico analysis of sortase superfamily.Journal of microbiology (Seoul, Korea) · 2019Article
- Quercetin impairs Streptococcus pneumoniae biofilm formation by inhibiting sortase A activity.Journal of cellular and molecular medicine · 2018Article
- NMR structure-based optimization of Staphylococcus aureus sortase A pyridazinone inhibitors.Chemical biology & drug design · 2017Article
- Structure and specificity of a new class of CaThe Journal of biological chemistry · 2017Article
- Sortase Transpeptidases: Structural Biology and Catalytic Mechanism.Advances in protein chemistry and structural biology · 2017Review
- The PRE-Derived NMR Model of the 38.8-kDa Tri-Domain IsdH Protein from Staphylococcus aureus Suggests That It Adaptively Recognizes Human Hemoglobin.Journal of molecular biology · 2016Article
- Structure of the Bacillus anthracis Sortase A Enzyme Bound to Its Sorting Signal: A FLEXIBLE AMINO-TERMINAL APPENDAGE MODULATES SUBSTRATE ACCESS.The Journal of biological chemistry · 2015Article
- Structural and biochemical analyses of a Clostridium perfringens sortase D transpeptidase.Acta crystallographica. Section D, Biological crystallography · 2015Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
The pathogen Bacillus anthracis uses the Sortase A (SrtA) enzyme to anchor proteins to its cell wall envelope during vegetative growth. To gain insight into the mechanism of protein attachment to the cell wall in B. anthracis we investigated the structure, backbone dynamics, and function of SrtA. The NMR structure of SrtA has been determined with a backbone coordinate precision of 0.40 +/- 0.07 A. SrtA possesses several novel features not previously observed in sortase enzymes including the presence of a structurally ordered amino terminus positioned within the active site and in contact with catalytically essential histidine residue (His(126)). We propose that this appendage, in combination with a unique flexible active site loop, mediates the recognition of lipid II, the second substrate to which proteins are attached during the anchoring reaction. pK(a) measurements indicate that His(126) is uncharged at physiological pH compatible with the enzyme operating through a "reverse protonation" mechanism. Interestingly, NMR relaxation measurements and the results of a model building study suggest that SrtA recognizes the LPXTG sorting signal through a lock-in-key mechanism in contrast to the prototypical SrtA enzyme from Staphylococcus aureus.
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Registered trials
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.