1v0e
From Proteopedia
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| - | [[Image:1v0e.jpg|left|200px]] | + | [[Image:1v0e.jpg|left|200px]] |
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| - | '''ENDOSIALIDASE OF BACTERIOPHAGE K1F''' | + | {{Structure |
| + | |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> | ||
| + | |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] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''ENDOSIALIDASE OF BACTERIOPHAGE K1F''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1V0E is a [ | + | 1V0E is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Xanthomonas_phage_cf16 Xanthomonas phage cf16]. 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:// | + | 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: Single protein]] | [[Category: Single protein]] | ||
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[[Category: polysialic acid degradation]] | [[Category: polysialic acid degradation]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:39:21 2008'' |
Revision as of 12:39, 20 March 2008
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| , resolution 1.90Å | |||||||
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| Sites: | |||||||
| Ligands: | |||||||
| Activity: | Endo-alpha-sialidase, with EC number 3.2.1.129 | ||||||
| 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 Xanthomonas phage cf16. 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 Thu Mar 20 14:39:21 2008
