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| | <StructureSection load='2j44' size='340' side='right'caption='[[2j44]], [[Resolution|resolution]] 2.10Å' scene=''> | | <StructureSection load='2j44' size='340' side='right'caption='[[2j44]], [[Resolution|resolution]] 2.10Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2j44]] is a 1 chain structure with sequence from [http://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=2J44 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2J44 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2j44]] 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=2J44 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2J44 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=2j44 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2j44 OCA], [http://pdbe.org/2j44 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2j44 RCSB], [http://www.ebi.ac.uk/pdbsum/2j44 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2j44 ProSAT]</span></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=PRD_900009:alpha-maltotriose'>PRD_900009</scene>, <scene name='pdbligand=PRD_900010:alpha-maltotetraose'>PRD_900010</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=2j44 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2j44 OCA], [https://pdbe.org/2j44 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2j44 RCSB], [https://www.ebi.ac.uk/pdbsum/2j44 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2j44 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/PULA_STRPN PULA_STRPN] Virulence factor (By similarity). Involved in the degradation of glycogen of the mammalian host cells (PubMed:21565699). Hydrolyzes the alpha-1,6-branchpoints of glycogen (PubMed:20497336, PubMed:21565699). Hydrolyzes pullulan. Does not hydrolyze dextran (PubMed:20497336). Binds to mouse lung alveolar type II cells that are rich in glycogen stores. Is an alpha-glucan-specific carbohydrate-binding protein, which binds to amylose (pure alpha-(1,4)-linked glucose), amylopectin (alpha-(1,4)-linked glucose with alpha-(1,6) branch points), pullulan (linear polymer of mixed alpha-(1,4)- and alpha-(1,6)-linked glucose) and glycogen (similar to amylopectin with more frequent alpha-(1,6) branch points) in vitro. Does not bind to dextran (a linear polymer of alpha-(1,6)-linked glucose) (PubMed:17187076).[UniProtKB:A0A0H2ZL64]<ref>PMID:17187076</ref> <ref>PMID:20497336</ref> <ref>PMID:21565699</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Boraston, A B]] | |
| - | [[Category: Bueren, A Lammerts van]] | |
| - | [[Category: Burke, R D]] | |
| - | [[Category: Higgins, M]] | |
| - | [[Category: Wang, D]] | |
| - | [[Category: Carbohydrate-binding module]] | |
| - | [[Category: Glycogen binding]] | |
| - | [[Category: Pullulanase]] | |
| | [[Category: Streptococcus pneumoniae]] | | [[Category: Streptococcus pneumoniae]] |
| - | [[Category: Virulence]] | + | [[Category: Boraston AB]] |
| | + | [[Category: Burke RD]] |
| | + | [[Category: Higgins M]] |
| | + | [[Category: Lammerts van Bueren A]] |
| | + | [[Category: Wang D]] |
| Structural highlights
Function
PULA_STRPN Virulence factor (By similarity). Involved in the degradation of glycogen of the mammalian host cells (PubMed:21565699). Hydrolyzes the alpha-1,6-branchpoints of glycogen (PubMed:20497336, PubMed:21565699). Hydrolyzes pullulan. Does not hydrolyze dextran (PubMed:20497336). Binds to mouse lung alveolar type II cells that are rich in glycogen stores. Is an alpha-glucan-specific carbohydrate-binding protein, which binds to amylose (pure alpha-(1,4)-linked glucose), amylopectin (alpha-(1,4)-linked glucose with alpha-(1,6) branch points), pullulan (linear polymer of mixed alpha-(1,4)- and alpha-(1,6)-linked glucose) and glycogen (similar to amylopectin with more frequent alpha-(1,6) branch points) in vitro. Does not bind to dextran (a linear polymer of alpha-(1,6)-linked glucose) (PubMed:17187076).[UniProtKB:A0A0H2ZL64][1] [2] [3]
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 ability of pathogenic bacteria to recognize host glycans is often essential to their virulence. Here we report structure-function studies of previously uncharacterized glycogen-binding modules in the surface-anchored pullulanases from Streptococcus pneumoniae (SpuA) and Streptococcus pyogenes (PulA). Multivalent binding to glycogen leads to a strong interaction with alveolar type II cells in mouse lung tissue. X-ray crystal structures of the binding modules reveal a novel fusion of tandem modules into single, bivalent functional domains. In addition to indicating a structural basis for multivalent attachment, the structure of the SpuA modules in complex with carbohydrate provides insight into the molecular basis for glycogen specificity. This report provides the first evidence that intracellular lung glycogen may be a novel target of pathogenic streptococci and thus provides a rationale for the identification of the streptococcal alpha-glucan-metabolizing machinery as virulence factors.
Identification and structural basis of binding to host lung glycogen by streptococcal virulence factors.,van Bueren AL, Higgins M, Wang D, Burke RD, Boraston AB Nat Struct Mol Biol. 2007 Jan;14(1):76-84. Epub 2006 Dec 24. PMID:17187076[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ van Bueren AL, Higgins M, Wang D, Burke RD, Boraston AB. Identification and structural basis of binding to host lung glycogen by streptococcal virulence factors. Nat Struct Mol Biol. 2007 Jan;14(1):76-84. Epub 2006 Dec 24. PMID:17187076 doi:http://dx.doi.org/10.1038/nsmb1187
- ↑ Abbott DW, Higgins MA, Hyrnuik S, Pluvinage B, Lammerts van Bueren A, Boraston AB. The molecular basis of glycogen breakdown and transport in Streptococcus pneumoniae. Mol Microbiol. 2010 Jul 1;77(1):183-99. Epub 2010 May 19. PMID:20497336 doi:10.1111/j.1365-2958.2010.07199.x
- ↑ Lammerts van Bueren A, Ficko-Blean E, Pluvinage B, Hehemann JH, Higgins MA, Deng L, Ogunniyi AD, Stroeher UH, El Warry N, Burke RD, Czjzek M, Paton JC, Vocadlo DJ, Boraston AB. The conformation and function of a multimodular glycogen-degrading pneumococcal virulence factor. Structure. 2011 May 11;19(5):640-51. PMID:21565699 doi:10.1016/j.str.2011.03.001
- ↑ van Bueren AL, Higgins M, Wang D, Burke RD, Boraston AB. Identification and structural basis of binding to host lung glycogen by streptococcal virulence factors. Nat Struct Mol Biol. 2007 Jan;14(1):76-84. Epub 2006 Dec 24. PMID:17187076 doi:http://dx.doi.org/10.1038/nsmb1187
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