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| | <StructureSection load='3faw' size='340' side='right'caption='[[3faw]], [[Resolution|resolution]] 2.10Å' scene=''> | | <StructureSection load='3faw' size='340' side='right'caption='[[3faw]], [[Resolution|resolution]] 2.10Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3faw]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_agalactiae_coh1 Streptococcus agalactiae coh1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3FAW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3FAW FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3faw]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_agalactiae_COH1 Streptococcus agalactiae COH1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3FAW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3FAW FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</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]] 2.1Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3fax|3fax]]</div></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SAN_1346 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=342616 Streptococcus agalactiae COH1])</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=3faw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3faw OCA], [https://pdbe.org/3faw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3faw RCSB], [https://www.ebi.ac.uk/pdbsum/3faw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3faw 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=3faw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3faw OCA], [https://pdbe.org/3faw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3faw RCSB], [https://www.ebi.ac.uk/pdbsum/3faw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3faw ProSAT]</span></td></tr> |
| | </table> | | </table> |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Streptococcus agalactiae coh1]] | + | [[Category: Streptococcus agalactiae COH1]] |
| - | [[Category: Gourlay, L J]] | + | [[Category: Gourlay LJ]] |
| - | [[Category: Beta barrel]]
| + | |
| - | [[Category: Cell wall]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Peptidoglycan-anchor]]
| + | |
| - | [[Category: Secreted]]
| + | |
| - | [[Category: Tim barrel]]
| + | |
| Structural highlights
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
The group B streptococcus type I pullulanase (SAP) is a class 13 glycoside hydrolase that is anchored to the bacterial cell surface via a conserved C-terminal anchoring motif and involved in alpha-glucan degradation. Recent in vitro functional studies have shown that SAP is immunogenic in humans and that anti-SAP sera derived from immunized animals impair both group A and group B streptococcus pullulanase activities, suggesting that in vivo immunization with this antigen could prevent streptococcal colonization. To further investigate the putative role of SAP in bacterial pathogenesis, we carried out functional studies and found that recombinant SAP binds to human cervical epithelial cells. Furthermore, with a view of using SAP as a vaccine candidate, we present high-resolution crystal structure analyses of an N-terminally truncated form of SAP lacking the carbohydrate binding module but containing the catalytic domain and displaying glycosidase hydrolase activity, both in its apo form and in complex with maltotetraose, at resolutions of 2.1 and 2.4 A, respectively.
Group B streptococcus pullulanase crystal structures in the context of a novel strategy for vaccine development.,Gourlay LJ, Santi I, Pezzicoli A, Grandi G, Soriani M, Bolognesi M J Bacteriol. 2009 Jun;191(11):3544-52. Epub 2009 Mar 27. PMID:19329633[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Gourlay LJ, Santi I, Pezzicoli A, Grandi G, Soriani M, Bolognesi M. Group B streptococcus pullulanase crystal structures in the context of a novel strategy for vaccine development. J Bacteriol. 2009 Jun;191(11):3544-52. Epub 2009 Mar 27. PMID:19329633 doi:10.1128/JB.01755-08
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