Conformational Analysis of the Streptococcus pneumoniae Hyaluronate Lyase and Characterization of Its Hyaluronan-specific Carbohydrate-binding Module

Suits, M.D.L.; Pluvinage, B.; Law, Adrienne; Liu, Yan; Palma, Angelina S.; Chai, Wengang; Feizi, Ten; Boraston, A.B.

doi:10.1074/jbc.m114.578435

Cited by 22 publications

(30 citation statements)

References 56 publications

(74 reference statements)

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“…3). It comprises, from N to C terminus, a signal peptide, a family 70 CBM, a linker domain, an a-catalytic domain, a b-catalytic domain and an LPXTG motif [157]. It comprises, from N to C terminus, a signal peptide, a family 70 CBM, a linker domain, an a-catalytic domain, a b-catalytic domain and an LPXTG motif [157].…”

Section: Depolymerization Transport and Processing Of Gagsmentioning

confidence: 99%

“…The aand bcatalytic domains together constitute a family 8 PL catalytic domain that cleaves glycosidic bonds via belimination. The catalytic activity of Hyl has been extensively interrogated through mutagenesis [159,[161][162][163], structural investigations [157,162,[164][165][166][167], and molecular dynamics simulations [167,168]. It also exhibits slow activity against ChS [158].…”

Section: Depolymerization Transport and Processing Of Gagsmentioning

confidence: 99%

“…Hyl targets the b-(1?4) linkages in HA and, following an initial endolytic cleavage event, acts processively in an exolytic manner along the polysaccharide, releasing disaccharide units containing an unsaturated GlcA [154,[158][159][160]. The CBM of Hyl binds HA oligoand polysaccharides with a degree of polymerization (DP) of > 6 [157]. The catalytic activity of Hyl has been extensively interrogated through mutagenesis [159,[161][162][163], structural investigations [157,162,[164][165][166][167], and molecular dynamics simulations [167,168].…”

Section: Depolymerization Transport and Processing Of Gagsmentioning

confidence: 99%

“…It also exhibits slow activity against ChS [158]. 3) [157]. These revealed that the a-domain possesses a domain-spanning cleft, located near the interface with the b-domain, which is able to accommodate HA; complex opening and closing, twisting and bending motions of the catalytic cleft contribute to processivity.…”

Section: Depolymerization Transport and Processing Of Gagsmentioning

confidence: 99%

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Glycan‐metabolizing enzymes in microbe–host interactions: the Streptococcus pneumoniae paradigm

2018

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Streptococcus pneumoniae is a frequent colonizer of the upper airways; however, it is also an accomplished pathogen capable of causing life-threatening diseases. To colonize and cause invasive disease, this bacterium relies on a complex array of factors to mediate the host-bacterium interaction. The respiratory tract is rich in functionally important glycoconjugates that display a vast range of glycans, and, thus, a key component of the pneumococcus-host interaction involves an arsenal of bacterial carbohydrate-active enzymes to depolymerize these glycans and carbohydrate transporters to import the products. Through the destruction of host glycans, the glycan-specific metabolic machinery deployed by S. pneumoniae plays a variety of roles in the host-pathogen interaction. Here, we review the processing and metabolism of the major host-derived glycans, including N- and O-linked glycans, Lewis and blood group antigens, proteoglycans, and glycogen, as well as some dietary glycans. We discuss the role of these metabolic pathways in the S. pneumoniae-host interaction, speculate on the potential of key enzymes within these pathways as therapeutic targets, and relate S. pneumoniae as a model system to glycan processing in other microbial pathogens.

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Section: Depolymerization Transport and Processing Of Gagsmentioning

confidence: 99%

Section: Depolymerization Transport and Processing Of Gagsmentioning

confidence: 99%

Section: Depolymerization Transport and Processing Of Gagsmentioning

confidence: 99%

Section: Depolymerization Transport and Processing Of Gagsmentioning

confidence: 99%

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Glycan‐metabolizing enzymes in microbe–host interactions: the Streptococcus pneumoniae paradigm

2018

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“…1). In general, high-resolution X-ray crystal structures of the individual modules are fit into the low-resolution SAXS molecular envelopes (~12-20 Å) generating pseudo-atomic resolution models of the ultra multimodular enzymes and their complexes [8][9][10][11]. Determining ultra multimodular protein structures using the combination of XRC and SAXS is an emerging frontier in structural biology research, providing important fundamental insights into full-length CAZymes with industrial, biomedical, and environmental significance.…”

Section: Introductionmentioning

confidence: 99%

Probing the Complex Architecture of Multimodular Carbohydrate-Active Enzymes Using a Combination of Small Angle X-Ray Scattering and X-Ray Crystallography

Czjzek¹,

Ficko-Blean²

2017

Methods in Molecular Biology

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The various modules in multimodular carbohydrate-active enzymes (CAZymes) may function in catalysis, carbohydrate binding, protein-protein interactions or as linkers. Here, we describe how combining the biophysical techniques of Small Angle X-ray Scattering (SAXS) and macromolecular X-ray crystallography (XRC) provides a powerful tool for examination into questions related to overall structural organization of ultra multimodular CAZymes.

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Hyaluronan‐protein interactions: Lilliput revisited

Day

2024

Proteoglycan Research

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Hyaluronan (HA) is a huge linear polysaccharide composed entirely of a simple repeating disaccharide that has been preserved unchanged since the evolution of vertebrates ~520 million years ago. It is present in all mammalian tissues, being synthesised within the cell membrane and extruded into the extracellular space where it dictates tissue elasticity, hydration and permeability. HA also directs cell behaviour via engagement with cell surface receptors. These properties allow it to mediate diverse functions in a wide range of physiological and pathological processes, including development, mammalian reproduction and inflammation. There is growing evidence that the way in which the HA biopolymer is differentially organised, through its interaction with a repertoire of HA‐binding proteins (HABPs), is key to the diversity of its biological functions. This review summarises current knowledge of HA‐protein interactions and how their diversity may lead to the formation of HA/protein complexes with distinct molecular architectures that in turn underpin different physical properties and receptor‐mediated effects. Potentially controversial areas such the pro‐inflammatory effects of low molecular weight HA fragments and how short HA‐binding peptides modulate HA function are considered from a molecular perspective.

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Conformational Analysis of the Streptococcus pneumoniae Hyaluronate Lyase and Characterization of Its Hyaluronan-specific Carbohydrate-binding Module

Cited by 22 publications

References 56 publications

Glycan‐metabolizing enzymes in microbe–host interactions: the Streptococcus pneumoniae paradigm

Glycan‐metabolizing enzymes in microbe–host interactions: the Streptococcus pneumoniae paradigm

Probing the Complex Architecture of Multimodular Carbohydrate-Active Enzymes Using a Combination of Small Angle X-Ray Scattering and X-Ray Crystallography

Hyaluronan‐protein interactions: Lilliput revisited

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