4d0q: Difference between revisions

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<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4d0q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4d0q OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4d0q RCSB], [http://www.ebi.ac.uk/pdbsum/4d0q PDBsum]</span></td></tr>

<table>

== Publication Abstract from PubMed ==

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 A resolution X-ray crystal structure of CBM70 revealed it to have a beta-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 (SAXS) revealed the full-length Hyl protein to exist as a monomer-dimer mixture in solution. Through a detailed analysis of the SAXS data we report the pseudo-atomic solution structures of the monomer and dimer forms of the full-length multimodular Hyl.

Conformational analysis of the Streptococcus pneumoniae hyaluronate lyase and characterization of its hyaluronan-specific carbohydrate-binding module.,Suits MD, Pluvinage B, Law A, Liu Y, Palma AS, Chai W, Feizi T, Boraston AB J Biol Chem. 2014 Aug 6. pii: jbc.M114.578435. PMID:25100731<ref>PMID:25100731</ref>

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>

</div>

== References ==

__TOC__

</StructureSection>

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@@ Line 7: / Line 7: @@
 <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4d0q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4d0q OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4d0q RCSB], [http://www.ebi.ac.uk/pdbsum/4d0q PDBsum]</span></td></tr>
 <table>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+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 A resolution X-ray crystal structure of CBM70 revealed it to have a beta-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 (SAXS) revealed the full-length Hyl protein to exist as a monomer-dimer mixture in solution. Through a detailed analysis of the SAXS data we report the pseudo-atomic solution structures of the monomer and dimer forms of the full-length multimodular Hyl.
+Conformational analysis of the Streptococcus pneumoniae hyaluronate lyase and characterization of its hyaluronan-specific carbohydrate-binding module.,Suits MD, Pluvinage B, Law A, Liu Y, Palma AS, Chai W, Feizi T, Boraston AB J Biol Chem. 2014 Aug 6. pii: jbc.M114.578435. PMID:25100731<ref>PMID:25100731</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+== References ==
+<references/>
 __TOC__
 </StructureSection>