1v0e
From Proteopedia
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|PDB= 1v0e |SIZE=350|CAPTION= <scene name='initialview01'>1v0e</scene>, resolution 1.90Å | |PDB= 1v0e |SIZE=350|CAPTION= <scene name='initialview01'>1v0e</scene>, resolution 1.90Å | ||
|SITE= <scene name='pdbsite=AC1:Po4+Binding+Site+For+Chain+D'>AC1</scene> | |SITE= <scene name='pdbsite=AC1:Po4+Binding+Site+For+Chain+D'>AC1</scene> | ||
| - | |LIGAND= <scene name='pdbligand=PO4:PHOSPHATE ION'>PO4</scene> | + | |LIGAND= <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene> |
| - | |ACTIVITY= [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] | + | |ACTIVITY= <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> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1v0e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1v0e OCA], [http://www.ebi.ac.uk/pdbsum/1v0e PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1v0e RCSB]</span> | ||
}} | }} | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1V0E is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/ | + | 1V0E is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Enterobacteria_phage_k1f Enterobacteria phage k1f]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1V0E OCA]. |
==Reference== | ==Reference== | ||
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:[http://www.ncbi.nlm.nih.gov/pubmed/15608653 15608653] | 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:[http://www.ncbi.nlm.nih.gov/pubmed/15608653 15608653] | ||
[[Category: Endo-alpha-sialidase]] | [[Category: Endo-alpha-sialidase]] | ||
| + | [[Category: Enterobacteria phage k1f]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Xanthomonas phage cf16]] | ||
[[Category: Dickmanns, A.]] | [[Category: Dickmanns, A.]] | ||
[[Category: Ficner, R.]] | [[Category: Ficner, R.]] | ||
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[[Category: Muehlenhoff, M.]] | [[Category: Muehlenhoff, M.]] | ||
[[Category: Stummeyer, K.]] | [[Category: Stummeyer, K.]] | ||
| - | [[Category: PO4]] | ||
[[Category: endosialidase]] | [[Category: endosialidase]] | ||
[[Category: glycosidase.]] | [[Category: glycosidase.]] | ||
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[[Category: polysialic acid degradation]] | [[Category: polysialic acid degradation]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:17:52 2008'' |
Revision as of 21:17, 30 March 2008
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| , resolution 1.90Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | |||||||
| Ligands: | |||||||
| Activity: | Endo-alpha-sialidase, with EC number 3.2.1.129 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
ENDOSIALIDASE OF BACTERIOPHAGE K1F
Overview
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.
About this Structure
1V0E is a Single protein structure of sequence from Enterobacteria phage k1f. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Mon Mar 31 00:17:52 2008
