AI Article Synopsis
- The study focuses on the crystal structure of a periplasmic glucose-binding protein (GBP) from Thermotoga maritima, which is essential for understanding transport systems across various organisms.
- The structure reveals two similar α/β domains linked by a hinge region, with β-D-glucose ligand nestled between them in a closed conformation.
- Detailed analysis shows that ten residues form hydrogen bonds with the glucose, while four aromatic residues stabilize it, demonstrating how substrate specificity is achieved in these transport systems.
Article Abstract
ABC transport systems have been characterized in organisms ranging from bacteria to humans. In most bacterial systems, the periplasmic component is the primary determinant of specificity of the transport complex as a whole. Here, the X-ray crystal structure of a periplasmic glucose-binding protein (GBP) from Thermotoga maritima determined at 2.4 Å resolution is reported. The molecule consists of two similar α/β domains connected by a three-stranded hinge region. In the current structure, a ligand (β-D-glucose) is buried between the two domains, which have adopted a closed conformation. Details of the substrate-binding sites revealed features that determine substrate specificity. In toto, ten residues from both domains form eight hydrogen bonds to the bound sugar and four aromatic residues (two from each domain) stabilize the substrate through stacking interactions.
Download full-text PDF |
Source |
|---|---|
| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3509965 | PMC |
| http://dx.doi.org/10.1107/S1744309112045241 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
The Actinobacillus pleuropneumoniae apxIV operon encodes an antibacterial toxin-immunity pair.
Microbiol Res
December 2024
Institute of Microbiology of the Czech Academy of Sciences, Videnska 1083, Prague 142 00, Czech Republic. Electronic address:
The ApxIVA protein belongs to a distinct class of a "clip and link" activity of Repeat-in-ToXin (RTX) exoproteins. Along with the three other pore-forming RTX toxins (ApxI, ApxII and ApxIII), ApxIVA serves as a major virulence factor of Actinobacillus pleuropneumoniae, the causative agent of porcine pneumonia. The gene encoding ApxIVA is located on a bicistronic operon downstream of the orf1 gene and is expressed exclusively under in vivo conditions.
View Article and Find Full Text PDFDeciphering the molecular basis of lipoprotein recognition and transport by LolCDE.
Signal Transduct Target Ther
December 2024
Department of Laboratory Medicine, State Key Laboratory of Biotherapy, National Clinical Research Center for Geriatrics, West China Hospital, Sichuan University and Collaborative Innovation Center of Biotherapy, Chengdu, China.
Outer membrane (OM) lipoproteins serve vital roles in Gram-negative bacteria, contributing to their pathogenicity and drug resistance. For these lipoproteins to function, they must be transported from the inner membrane (IM), where they are assembled, to the OM by the ABC transporter LolCDE. We have previously captured structural snapshots of LolCDE in multiple states, revealing its dynamic conformational changes.
View Article and Find Full Text PDFConformational changes in and translocation of small proteins: insights into the ejection mechanism of podophages.
J Virol
December 2024
Institute of Interdisciplinary Studies, Key Laboratory for Matter Microstructure and Function of Hunan Province, Key Laboratory of Low-dimensional Quantum Structures and Quantum Control, School of Physics and Electronics, Hunan Normal University, Changsha, China.
Unlabelled: Podophage tails are too short to span the cell envelope during infection. Consequently, podophages initially eject the core proteins within the head for the formation of an elongated trans-envelope channel for DNA ejection. Although the core proteins of bacteriophage T7 have been resolved at near-atomic resolution, the mechanisms of core proteins and DNA ejection remain to be fully elucidated.
View Article and Find Full Text PDFComparative proteomic analysis to annotate the structural association of the hypothetical proteins from the conserved domain of P. aeruginosa as novel vaccine candidates.
Biotechnol Lett
December 2024
Department of Bioinformatics, BioNome, Bengaluru, Karnataka, 560043, India.
Objectives: Pseudomonas aeruginosa, identified as an ESKAPE pathogen, contributes to severe clinical diseases worldwide and despite its prevalence an effective vaccine or treatment remains elusive. Numerous computational methods are being employed to target hypothetical proteins (HPs). Presently, no studies have predicted multi-epitope vaccines for these HPs.
View Article and Find Full Text PDFUnveiling the versatility of the thioredoxin framework: Insights from the structural examination of DsbA1.
Comput Struct Biotechnol J
December 2024
Department of Biochemistry and Chemistry, La Trobe Institute for Molecular Science, School of Agriculture, Biomedicine and Environment, La Trobe University, Bundoora, Australia.
In bacteria the formation of disulphide bonds is facilitated by a family of enzymes known as the disulphide bond forming (Dsb) proteins, which, despite low sequence homology, belong to the thioredoxin (TRX) superfamily. Among these enzymes is the disulphide bond-forming protein A (DsbA); a periplasmic thiol oxidase responsible for catalysing the oxidative folding of numerous cell envelope and secreted proteins. Pathogenic bacteria often contain diverse Dsb proteins with distinct functionalities commonly associated with pathogenesis.
View Article and Find Full Text PDFWant AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!