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| | <StructureSection load='1f9g' size='340' side='right'caption='[[1f9g]], [[Resolution|resolution]] 2.00Å' scene=''> | | <StructureSection load='1f9g' size='340' side='right'caption='[[1f9g]], [[Resolution|resolution]] 2.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1f9g]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"diplococcus_pneumoniae"_(klein_1884)_weichselbaum_1886 "diplococcus pneumoniae" (klein 1884) weichselbaum 1886]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F9G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1F9G FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1f9g]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_pneumoniae Streptococcus pneumoniae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F9G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1F9G FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ASC:ASCORBIC+ACID'>ASC</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1egu|1egu]], [[1f1s|1f1s]]</div></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ASC:ASCORBIC+ACID'>ASC</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Hyaluronate_lyase Hyaluronate lyase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.2.1 4.2.2.1] </span></td></tr>
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| | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1f9g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f9g OCA], [https://pdbe.org/1f9g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1f9g RCSB], [https://www.ebi.ac.uk/pdbsum/1f9g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1f9g ProSAT]</span></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=1f9g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f9g OCA], [https://pdbe.org/1f9g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1f9g RCSB], [https://www.ebi.ac.uk/pdbsum/1f9g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1f9g ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/HYSA_STRPN HYSA_STRPN] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Hyaluronate lyase]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Jedrzejas, M J]] | + | [[Category: Streptococcus pneumoniae]] |
| - | [[Category: Li, S]] | + | [[Category: Jedrzejas MJ]] |
| - | [[Category: Ascorbic acid binds to the indole group of trp292]] | + | [[Category: Li S]] |
| - | [[Category: Lyase]]
| + | |
| - | [[Category: Transmembrane]]
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| Structural highlights
Function
HYSA_STRPN
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Enzyme activity measurement showed that L-ascorbic acid (vitamin C (Vc)) competitively inhibits the hyaluronan degradation by Streptococcus pneumoniae hyaluronate lyase. The complex crystal structure of this enzyme with Vc was determined at 2.0 A resolution. One Vc molecule was found to bind to the active site of the enzyme. The Vc carboxyl group provides the negative charges that lead the molecule into the highly positively charged cleft of the enzyme. The Vc ring system forms hydrophobic interactions with the side chain of Trp-292, which is one of the aromatic patch residues of this enzyme responsible for the selection of the cleavage sites on the substrate chain. The binding of Vc inhibits the substrate binding at hyaluronan 1, 2, and 3 (HA1, HA2, and HA3) catalytic positions. The high concentration of Vc in human tissues probably provides a low level of natural resistance to the pneumococcal invasion. This is the first time that Vc the direct inhibition on the bacterial "spreading factor" was reported, and Vc is also the first chemical that has been shown experimentally to have an inhibitory effect on bacterial hyaluronate lyase. These studies also highlight the possible structural requirement for the design of a stronger inhibitor of bacterial hyaluronate lyase.
Vitamin C inhibits the enzymatic activity of Streptococcus pneumoniae hyaluronate lyase.,Li S, Taylor KB, Kelly SJ, Jedrzejas MJ J Biol Chem. 2001 May 4;276(18):15125-30. Epub 2001 Jan 12. PMID:11278838[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Li S, Taylor KB, Kelly SJ, Jedrzejas MJ. Vitamin C inhibits the enzymatic activity of Streptococcus pneumoniae hyaluronate lyase. J Biol Chem. 2001 May 4;276(18):15125-30. Epub 2001 Jan 12. PMID:11278838 doi:10.1074/jbc.M011102200
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