ArticleProtein science : a publication of the Protein Society2013
Structural characterization of Staphylococcus aureus biotin protein ligase and interaction partners: an antibiotic target.
Article in Protein science : a publication of the Protein Society, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 40 citations in OpenAlex.
- Bioorthogonal Click Chemistry for Antibody-Free Profiling of Acetylation, Propionylation, and Butyrylation inACS infectious diseases · 2026Article
- Hydrogen-Deuterium Exchange Defines Ligand-Induced Conformational Changes to the Class III Biotin Protein Ligase from Saccharomyces cerevisiae.Chembiochem : a European journal of chemical biology · 2025Article
- Pathogenic bacteria enriched in the oral microbiota might be associated with recurrent pulmonary infections in elderly individuals.Aging clinical and experimental research · 2025Article
- New Potent Sulfonamide-Based Inhibitors ofACS medicinal chemistry letters · 2024Article
- Biotin protein ligase as you like it: Either extraordinarily specific or promiscuous protein biotinylation.Proteins · 2024Review
- Structural Study of Potent Triazole-Based Inhibitors ofACS medicinal chemistry letters · 2023Article
- Emergence of allostery through reorganization of protein residue network architecture.The Journal of chemical physics · 2023Article
- Advanced Resistance Studies Identify Two Discrete Mechanisms inAntibiotics (Basel, Switzerland) · 2020Article
- The Biotin Biosynthetic Pathway in Mycobacterium tuberculosis is a Validated Target for the Development of Antibacterial Agents.Current medicinal chemistry · 2020Review
- A Novel Lipoate-Protein Ligase, Mhp-LplJ, Is Required for Lipoic Acid Metabolism inFrontiers in microbiology · 2020Article
- Strain-Specific Metabolic Requirements Revealed by a Defined Minimal Medium for Systems Analyses ofApplied and environmental microbiology · 2019Article
- Native mass spectrometry identifies an alternative DNA-binding pathway for BirA from Staphylococcus aureus.Scientific reports · 2019Article
- Specificity and selectivity in post-translational biotin addition.Biochemical Society transactions · 2018Review
- A conserved regulatory mechanism in bifunctional biotin protein ligases.Protein science : a publication of the Protein Society · 2017Article
- New Series of BPL Inhibitors To Probe the Ribose-Binding Pocket ofACS medicinal chemistry letters · 2016Article
- Biotin Protein Ligase Is a Target for New Antibacterials.Antibiotics (Basel, Switzerland) · 2016Review
- Mechanisms of biotin-regulated gene expression in microbes.Synthetic and systems biotechnology · 2016Review
- Transcriptomic Analysis of Staphylococcus epidermidis Biofilm-Released Cells upon Interaction with Human Blood Circulating Immune Cells and Soluble Factors.Frontiers in microbiology · 2016Article
- Improved Synthesis of Biotinol-5'-AMP: Implications for Antibacterial Discovery.ACS medicinal chemistry letters · 2015Article
- Sequence-function relationships in folding upon binding.Protein science : a publication of the Protein Society · 2015Article
Corrections and comments
- Erratum issuedTraore, D A K [added]
Authors and funding
10 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The essential metabolic enzyme biotin protein ligase (BPL) is a potential target for the development of new antibiotics required to combat drug-resistant pathogens. Staphylococcus aureus BPL (SaBPL) is a bifunctional protein, possessing both biotin ligase and transcription repressor activities. This positions BPL as a key regulator of several important metabolic pathways. Here, we report the structural analysis of both holo- and apo-forms of SaBPL using X-ray crystallography. We also present small-angle X-ray scattering data of SaBPL in complex with its biotin-carboxyl carrier protein substrate as well as the SaBPL:DNA complex that underlies repression. This has revealed the molecular basis of ligand (biotinyl-5'-AMP) binding and conformational changes associated with catalysis and repressor function. These data provide new information to better understand the bifunctional activities of SaBPL and to inform future strategies for antibiotic discovery.
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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.