ArticleThe Journal of biological chemistry2009
Structural analysis of semi-specific oligosaccharide recognition by a cellulose-binding protein of thermotoga maritima reveals adaptations for functional diversification of the oligopeptide periplasmic binding protein fold.
Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
15 citing papers in PubMed, 30 citations in OpenAlex.
- Large-scale quaternary structural transitions underlie gain of function of SPOP cancer mutations.Molecular cell · 2026Article
- Evidence for rapid hydrolysis of shoot-derived sucrose using an ultrasensitive ratiometric matryoshka-type MGlucoMeter sensor.The Plant journal : for cell and molecular biology · 2026Article
- A highly conserved ABC transporter mediates cello-oligosaccharide uptake in the extremely thermophilic, lignocellulolytic bacteriumApplied and environmental microbiology · 2026Article
- Structural insights into xyloglucan recognition by an ABC transporter from a Gram-positive, thermophilic bacterium.bioRxiv : the preprint server for biology · 2025Article
- Periplasmic chitooligosaccharide-binding protein requires a three-domain organization for substrate translocation.Scientific reports · 2023Article
- Utilization of dietary mixed-linkage β-glucans by the Firmicute Blautia producta.The Journal of biological chemistry · 2023Article
- Characterization of a highly xylose tolerant β-xylosidase isolated from high temperature horse manure compost.BMC biotechnology · 2021Article
- Substrate adaptabilities of Thermotogae mannan binding proteins as a function of their evolutionary histories.Extremophiles : life under extreme conditions · 2016Article
- Composition, Assembly, and Trafficking of a Wheat Xylan Synthase Complex.Plant physiology · 2016Article
- Adaptive Evolution of Thermotoga maritima Reveals Plasticity of the ABC Transporter Network.Applied and environmental microbiology · 2015Article
- A Pyranose-2-Phosphate Motif Is Responsible for Both Antibiotic Import and Quorum-Sensing Regulation in Agrobacterium tumefaciens.PLoS pathogens · 2015Article
- Duplication of genes in an ATP-binding cassette transport system increases dynamic range while maintaining ligand specificity.The Journal of biological chemistry · 2014Article
- Molecular details of ligand selectivity determinants in a promiscuous β-glucan periplasmic binding protein.BMC structural biology · 2013Article
- Protein conformational switches: from nature to design.Chemistry (Weinheim an der Bergstrasse, Germany) · 2012Review
- Compensating stereochemical changes allow murein tripeptide to be accommodated in a conventional peptide-binding protein.The Journal of biological chemistry · 2011Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
Periplasmic binding proteins (PBPs) constitute a protein superfamily that binds a wide variety of ligands. In prokaryotes, PBPs function as receptors for ATP-binding cassette or tripartite ATP-independent transporters and chemotaxis systems. In many instances, PBPs bind their cognate ligands with exquisite specificity, distinguishing, for example, between sugar epimers or structurally similar anions. By contrast, oligopeptide-binding proteins bind their ligands through interactions with the peptide backbone but do not distinguish between different side chains. The extremophile Thermotoga maritima possesses a remarkable array of carbohydrate-processing metabolic systems, including the hydrolysis of cellulosic polymers. Here, we present the crystal structure of a T. maritima cellobiose-binding protein (tm0031) that is homologous to oligopeptide-binding proteins. T. maritima cellobiose-binding protein binds a variety of lengths of beta(1-->4)-linked glucose oligomers, ranging from two rings (cellobiose) to five (cellopentaose). The structure reveals that binding is semi-specific. The disaccharide at the nonreducing end binds specifically; the other rings are located in a large solvent-filled groove, where the reducing end makes several contacts with the protein, thereby imposing an upper limit of the oligosaccharides that are recognized. Semi-specific recognition, in which a molecular class rather than individual species is selected, provides an efficient solution for the uptake of complex mixtures.
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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.