1v0e
From Proteopedia
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| - | [[Image:1v0e. | + | [[Image:1v0e.jpg|left|200px]]<br /><applet load="1v0e" size="450" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1v0e" size="450" color="white" frame="true" align="right" spinBox="true" | + | |
caption="1v0e, resolution 1.90Å" /> | caption="1v0e, resolution 1.90Å" /> | ||
'''ENDOSIALIDASE OF BACTERIOPHAGE K1F'''<br /> | '''ENDOSIALIDASE OF BACTERIOPHAGE K1F'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1V0E is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Xanthomonas_phage_cf16 Xanthomonas phage cf16] with PO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] | + | 1V0E is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Xanthomonas_phage_cf16 Xanthomonas phage cf16] with PO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Known structural/functional Site: <scene name='pdbsite=AC1:Po4 Binding Site For Chain D'>AC1</scene>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1V0E OCA]. |
==Reference== | ==Reference== | ||
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[[Category: polysialic acid degradation]] | [[Category: polysialic acid degradation]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Dec 18 18:20:22 2007'' |
Revision as of 16:10, 18 December 2007
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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 with PO4 as ligand. Active as Endo-alpha-sialidase, with EC number 3.2.1.129 Known structural/functional Site: . 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
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