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| | <StructureSection load='1v0f' size='340' side='right'caption='[[1v0f]], [[Resolution|resolution]] 2.55Å' scene=''> | | <StructureSection load='1v0f' size='340' side='right'caption='[[1v0f]], [[Resolution|resolution]] 2.55Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1v0f]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Bpk1f Bpk1f]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1V0F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1V0F FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1v0f]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_phage_K1F Escherichia phage K1F]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1V0F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1V0F FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=SLB:5-N-ACETYL-BETA-D-NEURAMINIC+ACID'>SLB</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]] 2.55Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=SIA:O-SIALIC+ACID'>SIA</scene></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=SIA:O-SIALIC+ACID'>SIA</scene>, <scene name='pdbligand=SLB:5-N-ACETYL-BETA-D-NEURAMINIC+ACID'>SLB</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1v0e|1v0e]]</div></td></tr>
| + | |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Endo-alpha-sialidase Endo-alpha-sialidase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.129 3.2.1.129] </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=1v0f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1v0f OCA], [https://pdbe.org/1v0f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1v0f RCSB], [https://www.ebi.ac.uk/pdbsum/1v0f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1v0f 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=1v0f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1v0f OCA], [https://pdbe.org/1v0f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1v0f RCSB], [https://www.ebi.ac.uk/pdbsum/1v0f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1v0f ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/FIBER_BPK1F FIBER_BPK1F] Responsible for initial absorption of the phage to the host bacterium. Degrades the alpha-2,8-linked polysialic acid K1 capsule by cleaving within the polymer chain of polysialic acid.<ref>PMID:20096705</ref> <ref>PMID:3546309</ref> The C-terminal chaperone protein mediates homotrimerization and proper folding of the catalytic endo-N trimer.<ref>PMID:12556457</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bpk1f]] | + | [[Category: Escherichia phage K1F]] |
| - | [[Category: Endo-alpha-sialidase]]
| + | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Dickmanns, A]] | + | [[Category: Dickmanns A]] |
| - | [[Category: Ficner, R]] | + | [[Category: Ficner R]] |
| - | [[Category: Gerady-Schahn, R]] | + | [[Category: Gerady-Schahn R]] |
| - | [[Category: Muehlenhoff, M]] | + | [[Category: Muehlenhoff M]] |
| - | [[Category: Stummeyer, K]] | + | [[Category: Stummeyer K]] |
| - | [[Category: Endosialidase]]
| + | |
| - | [[Category: Glycosidase]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Polysialic acid degradation]]
| + | |
| Structural highlights
Function
FIBER_BPK1F Responsible for initial absorption of the phage to the host bacterium. Degrades the alpha-2,8-linked polysialic acid K1 capsule by cleaving within the polymer chain of polysialic acid.[1] [2] The C-terminal chaperone protein mediates homotrimerization and proper folding of the catalytic endo-N trimer.[3]
Publication Abstract from PubMed
Phages infecting the polysialic acid (polySia)-encapsulated human pathogen Escherichia coli K1 are equipped with capsule-degrading tailspikes known as endosialidases, which are the only identified enzymes that specifically degrade polySia. As polySia also promotes cellular plasticity and tumor metastasis in vertebrates, endosialidases are widely applied in polySia-related neurosciences and cancer research. Here we report the crystal structures of endosialidase NF and its complex with oligomeric sialic acid. The structure NF, which reveals three distinct domains, indicates that the unique polySia specificity evolved from a combination of structural elements characteristic of exosialidases and bacteriophage tailspike proteins. The endosialidase assembles into a catalytic trimer stabilized by a triple beta-helix. Its active site differs markedly from that of exosialidases, indicating an endosialidase-specific substrate-binding mode and catalytic mechanism. Residues essential for endosialidase activity were identified by structure-based mutational analysis.
Crystal structure of the polysialic acid-degrading endosialidase of bacteriophage K1F.,Stummeyer K, Dickmanns A, Muhlenhoff M, Gerardy-Schahn R, Ficner R Nat Struct Mol Biol. 2005 Jan;12(1):90-6. Epub 2004 Dec 19. PMID:15608653[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Schulz EC, Schwarzer D, Frank M, Stummeyer K, Muhlenhoff M, Dickmanns A, Gerardy-Schahn R, Ficner R. Structural basis for the recognition and cleavage of polysialic acid by the bacteriophage K1F tailspike protein EndoNF. J Mol Biol. 2010 Mar 19;397(1):341-51. Epub 2010 Jan 22. PMID:20096705 doi:10.1016/j.jmb.2010.01.028
- ↑ Hallenbeck PC, Vimr ER, Yu F, Bassler B, Troy FA. Purification and properties of a bacteriophage-induced endo-N-acetylneuraminidase specific for poly-alpha-2,8-sialosyl carbohydrate units. J Biol Chem. 1987 Mar 15;262(8):3553-61. PMID:3546309
- ↑ Muhlenhoff M, Stummeyer K, Grove M, Sauerborn M, Gerardy-Schahn R. Proteolytic processing and oligomerization of bacteriophage-derived endosialidases. J Biol Chem. 2003 Apr 11;278(15):12634-44. Epub 2003 Jan 29. PMID:12556457 doi:10.1074/jbc.M212048200
- ↑ Stummeyer K, Dickmanns A, Muhlenhoff M, Gerardy-Schahn R, Ficner R. Crystal structure of the polysialic acid-degrading endosialidase of bacteriophage K1F. Nat Struct Mol Biol. 2005 Jan;12(1):90-6. Epub 2004 Dec 19. PMID:15608653 doi:nsmb874
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