|
|
| Line 3: |
Line 3: |
| | <StructureSection load='5a6j' size='340' side='right'caption='[[5a6j]], [[Resolution|resolution]] 1.94Å' scene=''> | | <StructureSection load='5a6j' size='340' side='right'caption='[[5a6j]], [[Resolution|resolution]] 1.94Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5a6j]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Strpn Strpn]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5A6J OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5A6J FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5a6j]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_pneumoniae_TIGR4 Streptococcus pneumoniae TIGR4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5A6J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5A6J FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5a69|5a69]], [[5a6a|5a6a]], [[5a6b|5a6b]], [[5a6k|5a6k]]</td></tr>
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5a6j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5a6j OCA], [https://pdbe.org/5a6j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5a6j RCSB], [https://www.ebi.ac.uk/pdbsum/5a6j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5a6j ProSAT]</span></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Beta-N-acetylhexosaminidase Beta-N-acetylhexosaminidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.52 3.2.1.52] </span></td></tr>
| + | |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5a6j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5a6j OCA], [http://pdbe.org/5a6j PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5a6j RCSB], [http://www.ebi.ac.uk/pdbsum/5a6j PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5a6j ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/A0A0H2US73_STRPN A0A0H2US73_STRPN] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 18: |
Line 18: |
| | </div> | | </div> |
| | <div class="pdbe-citations 5a6j" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 5a6j" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Beta-N-acetylhexosaminidase 3D structures|Beta-N-acetylhexosaminidase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Beta-N-acetylhexosaminidase]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Strpn]] | + | [[Category: Streptococcus pneumoniae TIGR4]] |
| - | [[Category: Boraston, A B]] | + | [[Category: Boraston AB]] |
| - | [[Category: Cid, M]] | + | [[Category: Cid M]] |
| - | [[Category: Higgins, M A]] | + | [[Category: Higgins MA]] |
| - | [[Category: Robb, C S]] | + | [[Category: Robb CS]] |
| - | [[Category: Bacterial protein]]
| + | |
| - | [[Category: Beta-hexosaminidase]]
| + | |
| - | [[Category: Carbohydrate conformation]]
| + | |
| - | [[Category: Catalytic domain]]
| + | |
| - | [[Category: Host-pathogen interaction]]
| + | |
| - | [[Category: Hydrogen bonding]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Hydrolysis]]
| + | |
| - | [[Category: Model]]
| + | |
| - | [[Category: Polysaccharide]]
| + | |
| - | [[Category: Streptococcus pneumoniae]]
| + | |
| - | [[Category: Virulence factor]]
| + | |
| Structural highlights
Function
A0A0H2US73_STRPN
Publication Abstract from PubMed
An important facet of the interaction between the pathogen Streptococcus pneumoniae (pneumococcus) and its human host is the ability of this bacterium to process host glycans. To achieve cleavage of the glycosidic bonds in host glycans, S. pneumoniae deploys a wide array of glycoside hydrolases. Here, we identify and characterize a new family 20 glycoside hydrolase, GH20C, from S. pneumoniae. Recombinant GH20C possessed the ability to hydrolyze the beta-linkages joining either N-acetylglucosamine or N-acetylgalactosamine to a wide variety of aglycon residues, thus revealing this enzyme to be a generalist N-acetylhexosaminidase in vitro. X-ray crystal structures were determined for GH20C in a ligand-free form, in complex with the N-acetylglucosamine and N-acetylgalactosamine products of catalysis and in complex with both gluco- and galacto-configured inhibitors O-(2-acetamido-2-deoxy-D-glucopyranosylidene)amino N-phenyl carbamate (PUGNAc), O-(2-acetamido-2-deoxy-D-galactopyranosylidene)amino N-phenyl carbamate (GalPUGNAc), N-acetyl-D-glucosamine-thiazoline (NGT), and N-acetyl-D-galactosamine-thiazoline (GalNGT) at resolutions from 1.84 to 2.7 A. These structures showed N-acetylglucosamine and N-acetylgalactosamine to be recognized via identical sets of molecular interactions. Although the same sets of interaction were maintained with the gluco- and galacto-configured inhibitors, the inhibition constants suggested preferred recognition of the axial O4 when an aglycon moiety was present (Ki for PUGNAc > GalPUGNAc) but preferred recognition of an equatorial O4 when the aglycon was absent (Ki for GalNGT > NGT). Overall, this study reveals GH20C to be another tool that is unique in the arsenal of S. pneumoniae and that it may implement the effort of the bacterium to utilize and/or destroy the wide array of host glycans that it may encounter.
A Second beta-Hexosaminidase Encoded in the Streptococcus pneumoniae Genome Provides an Expanded Biochemical Ability to Degrade Host Glycans.,Robb M, Robb CS, Higgins MA, Hobbs JK, Paton JC, Boraston AB J Biol Chem. 2015 Dec 25;290(52):30888-900. doi: 10.1074/jbc.M115.688630. Epub, 2015 Oct 21. PMID:26491009[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Robb M, Robb CS, Higgins MA, Hobbs JK, Paton JC, Boraston AB. A Second beta-Hexosaminidase Encoded in the Streptococcus pneumoniae Genome Provides an Expanded Biochemical Ability to Degrade Host Glycans. J Biol Chem. 2015 Dec 25;290(52):30888-900. doi: 10.1074/jbc.M115.688630. Epub, 2015 Oct 21. PMID:26491009 doi:http://dx.doi.org/10.1074/jbc.M115.688630
|
