A5050102087- Bacterial Genetics and Biotechnology
- Enzyme Structure and Function
- Drug Transport and Resistance Mechanisms
- RNA and protein synthesis mechanisms
- Antibiotic Resistance in Bacteria
- Glycosylation and Glycoproteins Research
- Bacteriophages and microbial interactions
- Genomics and Phylogenetic Studies
- Protein Structure and Dynamics
- Radiopharmaceutical Chemistry and Applications
- Trace Elements in Health
- Radioactive element chemistry and processing
- Biochemical and Molecular Research
- Photosynthetic Processes and Mechanisms
- Veterinary medicine and infectious diseases
- Mass Spectrometry Techniques and Applications
- Chemical Analysis and Environmental Impact
- Chemical Synthesis and Characterization
- Pediatric Hepatobiliary Diseases and Treatments
- Antimicrobial Resistance in Staphylococcus
- Polyamine Metabolism and Applications
- Amoebic Infections and Treatments
- Metal-Catalyzed Oxygenation Mechanisms
- Molecular Biology Techniques and Applications
MacDiarmid Institute for Advanced Materials and Nanotechnology
2022-2024
Stockholm University
2023-2024
University of Canterbury
2017-2024
Maurice Wilkins Centre
2022-2024
Victor Chang Cardiac Research Institute
2024
Abstract In bacteria and archaea, tripartite ATP-independent periplasmic (TRAP) transporters uptake essential nutrients. TRAP receive their substrates via a secreted soluble substrate-binding protein. How sodium ion-driven secondary active transporter is strictly coupled to protein poorly understood. Here we report the cryo-EM structure of sialic acid SiaQM from Photobacterium profundum at 2.97 Å resolution. SiaM comprises “transport” domain “scaffold” domain, with transport consisting...
Tripartite ATP-independent periplasmic (TRAP) transporters are secondary-active that receive their substrates via a soluble-binding protein to move bioorganic acids across bacterial or archaeal cell membranes. Recent cryo-electron microscopy (cryo-EM) structures of TRAP provide broad framework understand how they work, but the mechanistic details transport not yet defined. Here we report cryo-EM structure Haemophilus influenzae N -acetylneuraminate transporter ( Hi SiaQM) at 2.99 Å...
Tripartite ATP-independent periplasmic (TRAP) transporters are secondary-active that receive their substrates via a soluble-binding protein to move bioorganic acids across bacterial or archaeal cell membranes. Recent cryo-electron microscopy (cryo-EM) structures of TRAP provide broad framework understand how they work, but the mechanistic details transport not yet defined. Here we report cryo-EM structure Haemophilus influenzae N-acetylneuraminate transporter (HiSiaQM) at 2.99 Å resolution...
N-Acetylglucosamine-6-phosphate deacetylase (NagA) and glucosamine-6-phosphate deaminase (NagB) are branch point enzymes that direct amino sugars into different pathways. For Staphylococcus aureus NagA, analytical ultracentrifugation small-angle X-ray scattering data demonstrate it is an asymmetric dimer in solution. Initial rate experiments show hysteresis, which may be related to pathway regulation, kinetic parameters similar other bacterial isozymes. The enzyme binds two Zn2+ ions not...
In environments where glucose is limited, some pathogenic bacteria metabolize host-derived sialic acid as a nutrient source. N-Acetylmannosamine kinase (NanK) the second enzyme of bacterial import and degradation pathway adds phosphate to N-acetylmannosamine using ATP prime molecule for future reactions. Sequence alignments reveal that Gram-positive NanK enzymes belong Repressor, ORF, Kinase (ROK) family, but many lack canonical Zn-binding motif expected this function, sugar-binding EXGH...
Human pathogenic and commensal bacteria have evolved the ability to scavenge host-derived sialic acids subsequently degrade them as a source of nutrition. Expression Escherichia coli yjhBC operon is controlled by repressor protein nanR, which regulates core machinery responsible for import catabolic processing acid. The role encoded proteins not known-here, we demonstrate that enzyme YjhC an oxidoreductase/dehydrogenase involved in bacterial acid degradation. First, vivo using knockout...
Tripartite ATP-independent periplasmic (TRAP) transporters are secondary-active that receive their substrates via a soluble binding protein to move bioorganic acids across bacterial or archaeal cell membranes. Recent cryo-EM structures of TRAP provide broad framework understand how they work, but the mechanistic details transport not yet defined. Here we report structure Haemophilus influenzae N -acetylneuraminate transporter ( Hi SiaQM) at 2.99 Å resolution (extending 2.2 core), revealing...
Abstract Tripartite ATP-independent periplasmic (TRAP) transporters are analogous to ABC in that they use a substrate-binding proteins scavenge metabolites ( e.g. , N -acetylneuraminate) and deliver them the membrane components for import. TRAP thought bind substrate using two-state (open closed) induced-fit mechanism. We solved structure of -acetylneuraminate protein from Aggregatibacter actinomycetemcomitans Aa SiaP) both open ligand-free closed liganded conformations. Surprisingly, we...
Abstract N ‐acetylglucosamine 6‐phosphate deacetylase (NagA) catalyzes the conversion of ‐acetylglucosamine‐6‐phosphate to glucosamine‐6‐phosphate in amino sugar catabolism. This is an essential step catabolism sialic acid several pathogenic bacteria, including Pasteurella multocida , and thus NagA identified as a potential drug target. Here, we report unique structural features from P. (PmNagA) resolved 1.95 Å. PmNagA displays altered quaternary architecture with interface interactions...
Tripartite ATP-independent periplasmic (TRAP) transporters are secondary-active that receive their substrates via a soluble binding protein to move bioorganic acids across bacterial or archaeal cell membranes. Recent cryo-EM structures of TRAP provide broad framework understand how they work, but the mechanistic details transport not yet defined. Here we report structure Haemophilus influenzae N -acetylneuraminate transporter ( Hi SiaQM) at 2.99 Å resolution (extending 2.2 core), revealing...
Bacteria evolve mechanisms to compete for limited resources and survive in new niches. Here we study the mechanism of isethionate import from sulfate-reducing bacterium Oleidesulfovibrio alaskensis. The catabolism by Desulfovibrio species has been implicated human disease, due hydrogen sulfide production, potential industrial applications. O. alaskensis employs a tripartite ATP-independent periplasmic (TRAP) transporter (OaIsePQM) isethionate, which relies on substrate-binding protein...
Abstract In bacteria and archaea, tripartite ATP-independent periplasmic (TRAP) transporters uptake essential carboxylate- sulfonate-containing nutrients into the cytoplasm. Unlike other secondary active transporters, TRAP cannot receive their substrates directly, but do so indirectly via a secreted soluble substrate-binding protein. How sodium-driven transporter is strictly coupled to passenger-carrying domain poorly understood. Here, we report cryo-EM structure of sialic acid SiaQM from...
Abstract Tripartite ATP-independent periplasmic (TRAP) transporters are secondary-active that receive their substrates via a soluble binding protein to move bioorganic acids across bacterial or archaeal cell membranes. Recent cryo-EM structures of TRAP provide broad framework understand how they work, but the mechanistic details transport not yet defined. Here we report structure Haemophilus influenzae N -acetylneuraminate transporter ( Hi SiaQM) at 2.99 Å resolution (extending 2.2 core),...