1v0e: Difference between revisions

Latest revision as of 09:07, 9 May 2024

Endosialidase of Bacteriophage K1F

Structural highlights

1v0e is a 6 chain structure with sequence from Escherichia phage K1F. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.9Å
Ligands:	PO4
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

[1] 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

[2] 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

[3] 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

[4] 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

[1]

[2]

[3]

[4]

@@ Line 3: / Line 3: @@
 <StructureSection load='1v0e' size='340' side='right'caption='[[1v0e]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1v0e]] 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=1V0E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1V0E FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1v0e]] 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=1V0E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1V0E 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></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]] 1.9&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1v0f|1v0f]]</div></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></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=1v0e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1v0e OCA], [https://pdbe.org/1v0e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1v0e RCSB], [https://www.ebi.ac.uk/pdbsum/1v0e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1v0e ProSAT]</span></td></tr>
 </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;">
 == Publication Abstract from PubMed ==
@@ Line 22: / Line 23: @@
 __TOC__
 </StructureSection>
-[[Category: Bpk1f]]
+[[Category: Escherichia phage K1F]]
-[[Category: Endo-alpha-sialidase]]
 [[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]]

1v0e: Difference between revisions

Latest revision as of 09:07, 9 May 2024

Endosialidase of Bacteriophage K1F

Structural highlights

Function

Publication Abstract from PubMed

References

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