Imperial College London
Alternate

DrWengangChai

Faculty of Medicine, Department of Metabolism, Digestion and Reproduction

Senior Research Fellow
 
 
 
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Contact

 

+44 (0)20 7594 2596w.chai

 
 
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Location

 

Burlington DanesHammersmith Campus

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Summary

 

Publications

Citation

BibTex format

@article{Suits:2014:10.1074/jbc.M114.578435,
author = {Suits, MDL and Pluvinage, B and Law, A and Liu, Y and Palma, AS and Chai, W and Feizi, T and Boraston, AB},
doi = {10.1074/jbc.M114.578435},
journal = {Journal of Biological Chemistry},
pages = {27264--27277},
title = {Conformational analysis of the Streptococcus pneumoniae hyaluronate lyase and characterization of Its hyaluronan-specific carbohydrate-binding module},
url = {http://dx.doi.org/10.1074/jbc.M114.578435},
volume = {289},
year = {2014}
}
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RIS format (EndNote, RefMan)

TY  - JOUR
AB  - For a subset of pathogenic microorganisms, including Streptococcus pneumoniae, the recognition and degradation of host hyaluronan contributes to bacterial spreading through the extracellular matrix and enhancing access to host cell surfaces. The hyaluronate lyase (Hyl) presented on the surface of S. pneumoniae performs this role. Using glycan microarray screening, affinity electrophoresis, and isothermal titration calorimetry we show that the N-terminal module of Hyl is a hyaluronan-specific carbohydrate-binding module (CBM) and the founding member of CBM family 70. The 1.2 Å resolution x-ray crystal structure of CBM70 revealed it to have a β-sandwich fold, similar to other CBMs. The electrostatic properties of the binding site, which was identified by site-directed mutagenesis, are distinct from other CBMs and complementary to its acidic ligand, hyaluronan. Dynamic light scattering and solution small angle x-ray scattering revealed the full-length Hyl protein to exist as a monomer/dimer mixture in solution. Through a detailed analysis of the small angle x-ray scattering data, we report the pseudoatomic solution structures of the monomer and dimer forms of the full-length multimodular Hyl.
AU  - Suits,MDL
AU  - Pluvinage,B
AU  - Law,A
AU  - Liu,Y
AU  - Palma,AS
AU  - Chai,W
AU  - Feizi,T
AU  - Boraston,AB
DO  - 10.1074/jbc.M114.578435
EP  - 27277
PY  - 2014///
SN  - 0021-9258
SP  - 27264
TI  - Conformational analysis of the Streptococcus pneumoniae hyaluronate lyase and characterization of Its hyaluronan-specific carbohydrate-binding module
T2  - Journal of Biological Chemistry
UR  - http://dx.doi.org/10.1074/jbc.M114.578435
UR  - http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcApp=PARTNER_APP&SrcAuth=LinksAMR&KeyUT=WOS:000342853900048&DestLinkType=FullRecord&DestApp=ALL_WOS&UsrCustomerID=1ba7043ffcc86c417c072aa74d649202
UR  - http://hdl.handle.net/10044/1/58361
VL  - 289
ER  -
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