Recognition of cellooligosaccharides by a family 28 carbohydrate‐binding module

Tsukimoto, K.; Takada, Ritsuko; Araki, Yuko; Suzuki, Kentaro; Karita, Shuichi; Wakagi, Takayoshi; Shoun, Hirofumi; Watanabe, Takashi; Fushinobu, Shinya

doi:10.1016/j.febslet.2010.02.027

Cited by 24 publications

(18 citation statements)

References 24 publications

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“…1A ). The backbone is flat, with less of the “twisted-ribbon” geometry observed in some cello- and xylogluco-oligosaccharides ( 34 – 36 ). The aromatic platform created by W330, W364, and Y363 spans four glucosyl residues, compared to the longer platform of SGBP-A, which supports six glucosyl residues ( Fig.…”

Section: Resultsmentioning

confidence: 99%

Molecular Dissection of Xyloglucan Recognition in a Prominent Human Gut Symbiont

Tauzin

Kwiatkowski

Orlovsky

et al. 2016

mBio

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Polysaccharide utilization loci (PUL) within the genomes of resident human gut Bacteroidetes are central to the metabolism of the otherwise indigestible complex carbohydrates known as “dietary fiber.” However, functional characterization of PUL lags significantly behind sequencing efforts, which limits physiological understanding of the human-bacterial symbiosis. In particular, the molecular basis of complex polysaccharide recognition, an essential prerequisite to hydrolysis by cell surface glycosidases and subsequent metabolism, is generally poorly understood. Here, we present the biochemical, structural, and reverse genetic characterization of two unique cell surface glycan-binding proteins (SGBPs) encoded by a xyloglucan utilization locus (XyGUL) from Bacteroides ovatus, which are integral to growth on this key dietary vegetable polysaccharide. Biochemical analysis reveals that these outer membrane-anchored proteins are in fact exquisitely specific for the highly branched xyloglucan (XyG) polysaccharide. The crystal structure of SGBP-A, a SusD homolog, with a bound XyG tetradecasaccharide reveals an extended carbohydrate-binding platform that primarily relies on recognition of the β-glucan backbone. The unique, tetra-modular structure of SGBP-B is comprised of tandem Ig-like folds, with XyG binding mediated at the distal C-terminal domain. Despite displaying similar affinities for XyG, reverse-genetic analysis reveals that SGBP-B is only required for the efficient capture of smaller oligosaccharides, whereas the presence of SGBP-A is more critical than its carbohydrate-binding ability for growth on XyG. Together, these data demonstrate that SGBP-A and SGBP-B play complementary, specialized roles in carbohydrate capture by B. ovatus and elaborate a model of how vegetable xyloglucans are accessed by the Bacteroidetes.

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Section: Resultsmentioning

confidence: 99%

Molecular Dissection of Xyloglucan Recognition in a Prominent Human Gut Symbiont

Tauzin

Kwiatkowski

Orlovsky

et al. 2016

mBio

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“…The production of cellulose oligomers by enzymatic depolymerization faces the difficulty that they appear in the early stage of the hydrolysis 85 and are then easily further hydrolysed. 54,86 For example, the exoglucanase cellobiohydrolase II was found to degrade cellulose oligomers with different rate depending on their size as follow: cellohexaose > cellotetraose > cellopentaose > cellotriose. 87 The main product of enzymatic depolymerization is generally cellobiose, as highlighted in Table 2, which is an enzyme inhibitor.…”

Section: Enzymatic Depolymerizationmentioning

confidence: 99%

Water-soluble cellulose oligomer production by chemical and enzymatic synthesis: a mini-review

et al. 2017

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This mini‐review focuses on the production of water‐soluble cellulose oligomers. They are easier to handle than cellulose while still having some very interesting cellulose features. Their production is not trivial and they are thus seldom commercially available or are available at high prices and only in small quantities (100 mg or less). The goal of this mini‐review is to describe various routes to obtain these cellulose oligomers. Several examples of chemical or enzymatic synthesis and enzymatic or acidic depolymerization are presented. All the pathways considered are then compared according to several criteria: polymerization degree, yield, availability and cost of reagents, reaction time, etc. As most of the pathways produce a mixture of cellulose oligomers, techniques to separate them according to their length are also discussed. © 2017 Society of Chemical Industry

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“…Although there are numerous published structures of type-B CBMs complexed with cellooligosaccharides (8)(9)(10)(11)(12), analogous structures for type-A CBMs have proved difficult to produce, and so the current concept of type-A CBM interaction with cellulose is based on indirect evidence. The current hypothesis, that type-A CBMs bind to the hydrophobic face of crystalline cellulose, stems from the observation that they have an open surface with a planar strip of aromatic residues suitably positioned to bind the planar surface of the aligned pyranose rings in crystalline cellulose (4,13).…”

mentioning

confidence: 99%

Structural basis for entropy-driven cellulose binding by a type-A cellulose-binding module (CBM) and bacterial expansin

Georgelis¹,

Yennawar

Cosgrove³

2012

Proc. Natl. Acad. Sci. U.S.A.

165

151

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Components of modular cellulases, type-A cellulose-binding modules (CBMs) bind to crystalline cellulose and enhance enzyme effectiveness, but structural details of the interaction are uncertain. We analyzed cellulose binding by EXLX1, a bacterial expansin with ability to loosen plant cell walls and whose domain D2 has type-A CBM characteristics. EXLX1 strongly binds to crystalline cellulose via D2, whereas its affinity for soluble cellooligosaccharides is weak. Calorimetry indicated cellulose binding was largely entropically driven. We solved the crystal structures of EXLX1 complexed with cellulose-like oligosaccharides to find that EXLX1 binds the ligands through hydrophobic interactions of three linearly arranged aromatic residues in D2. The crystal structures revealed a unique form of ligand-mediated dimerization, with the oligosaccharide sandwiched between two D2 domains in opposite polarity. This report clarifies the molecular target of expansin and the specific molecular interactions of a type-A CBM with cellulose.plant cell wall | X-ray crystallography

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Recognition of cellooligosaccharides by a family 28 carbohydrate‐binding module

Cited by 24 publications

References 24 publications

Molecular Dissection of Xyloglucan Recognition in a Prominent Human Gut Symbiont

Molecular Dissection of Xyloglucan Recognition in a Prominent Human Gut Symbiont

Water-soluble cellulose oligomer production by chemical and enzymatic synthesis: a mini-review

Structural basis for entropy-driven cellulose binding by a type-A cellulose-binding module (CBM) and bacterial expansin

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