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| | <StructureSection load='3ju4' size='340' side='right'caption='[[3ju4]], [[Resolution|resolution]] 0.98Å' scene=''> | | <StructureSection load='3ju4' size='340' side='right'caption='[[3ju4]], [[Resolution|resolution]] 0.98Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3ju4]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bpk1f Bpk1f]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3JU4 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=3JU4 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3ju4]] is a 1 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=3JU4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3JU4 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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]] 0.98Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1v0e|1v0e]], [[1v0f|1v0f]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=SLB:5-N-ACETYL-BETA-D-NEURAMINIC+ACID'>SLB</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Endo-alpha-sialidase Endo-alpha-sialidase], with EC number [http://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=3ju4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ju4 OCA], [https://pdbe.org/3ju4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ju4 RCSB], [https://www.ebi.ac.uk/pdbsum/3ju4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ju4 ProSAT]</span></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=3ju4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ju4 OCA], [http://pdbe.org/3ju4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3ju4 RCSB], [http://www.ebi.ac.uk/pdbsum/3ju4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3ju4 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> |
| | == 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: Bpk1f]] | + | [[Category: Escherichia phage K1F]] |
| - | [[Category: Endo-alpha-sialidase]]
| + | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Ficner, R]] | + | [[Category: Ficner R]] |
| - | [[Category: Gerardy-Schahn, R]] | + | [[Category: Gerardy-Schahn R]] |
| - | [[Category: Neuman, P]] | + | [[Category: Neuman P]] |
| - | [[Category: Schulz, E C]] | + | [[Category: Schulz EC]] |
| - | [[Category: Sheldrick, G M]] | + | [[Category: Sheldrick GM]] |
| - | [[Category: Endonf]]
| + | |
| - | [[Category: Glycosidase]]
| + | |
| - | [[Category: High-resolution]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Polysia]]
| + | |
| 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]
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
Endosialidase NF (endoNF) is a bacteriophage-derived endosialidase that specifically degrades alpha-2,8-linked polysialic acid. The structure of a new crystal form of endoNF in complex with sialic acid has been refined at 0.98 A resolution. The 210 kDa homotrimeric multi-domain enzyme displays outstanding stability and resistance to SDS. Even at atomic resolution, only a minor fraction of side chains possess alternative conformations. However, multiple conformations of an active-site residue imply that it has an important catalytic function in the cleavage mechanism of polysialic acid.
Structure analysis of endosialidase NF at 0.98 A resolution.,Schulz EC, Neumann P, Gerardy-Schahn R, Sheldrick GM, Ficner R Acta Crystallogr D Biol Crystallogr. 2010 Feb;66(Pt 2):176-80. Epub 2010 Jan 22. PMID:20124697[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
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
- ↑ Schulz EC, Neumann P, Gerardy-Schahn R, Sheldrick GM, Ficner R. Structure analysis of endosialidase NF at 0.98 A resolution. Acta Crystallogr D Biol Crystallogr. 2010 Feb;66(Pt 2):176-80. Epub 2010 Jan 22. PMID:20124697 doi:10.1107/S0907444909048720
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