ArticleThe Journal of biological chemistry2015
Structure of the Bacillus anthracis Sortase A Enzyme Bound to Its Sorting Signal: A FLEXIBLE AMINO-TERMINAL APPENDAGE MODULATES SUBSTRATE ACCESS.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 28 citations in OpenAlex.
- Conformational free energy landscape of sorting signal peptides in complex with bacterial sortases.Biophysical journal · 2026Article
- Amino Acid Variants at the P94 Position inBiochemistry · 2026Article
- Amino acid variants at the P94 position inbioRxiv : the preprint server for biology · 2026Article
- A Putative Interaction between the Transmembrane Domains ofThe journal of physical chemistry. B · 2025Article
- Discovery of a Potent Triazole-Based Reversible Targeted Covalent Inhibitor of Cruzipain.ACS medicinal chemistry letters · 2025Article
- A unique binding mode of P1' Leu-containing target sequences forRSC chemical biology · 2024Article
- The basal and major pilins in the Corynebacterium diphtheriae SpaA pilus adopt similar structures that competitively react with the pilin polymerase.Biopolymers · 2024Article
- Structural and biochemical analyses of selectivity determinants in chimeric Streptococcus Class A sortase enzymes.Protein science : a publication of the Protein Society · 2022Article
- Interrogation ofSaudi journal of biological sciences · 2021Article
- TheMicroorganisms · 2020Review
- Article
- Kinetics and Optimization of the Lysine-Isopeptide Bond Forming Sortase Enzyme fromBioconjugate chemistry · 2020Article
- Functional analysis ofThe Journal of biological chemistry · 2020Article
- A comprehensive in silico analysis of sortase superfamily.Journal of microbiology (Seoul, Korea) · 2019Article
- Sortase Transpeptidases: Structural Biology and Catalytic Mechanism.Advances in protein chemistry and structural biology · 2017Review
- The "Lid" in the Streptococcus pneumoniae SrtC1 Sortase Adopts a Rigid Structure that Regulates Substrate Access to the Active Site.The journal of physical chemistry. B · 2016Article
- Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
The endospore forming bacterium Bacillus anthracis causes lethal anthrax disease in humans and animals. The ability of this pathogen to replicate within macrophages is dependent upon the display of bacterial surface proteins attached to the cell wall by the B. anthracis Sortase A ((Ba)SrtA) enzyme. Previously, we discovered that the class A (Ba)SrtA sortase contains a unique N-terminal appendage that wraps around the body of the protein to contact the active site of the enzyme. To gain insight into its function, we determined the NMR structure of (Ba)SrtA bound to a LPXTG sorting signal analog. The structure, combined with dynamics, kinetics, and whole cell protein display data suggest that the N terminus modulates substrate access to the enzyme. We propose that it may increase the efficiency of protein display by reducing the unproductive hydrolytic cleavage of enzyme-protein covalent intermediates that form during the cell wall anchoring reaction. Notably, a key active site loop (β7/β8 loop) undergoes a disordered to ordered transition upon binding the sorting signal, potentially facilitating recognition of lipid II.
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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.