1v0e

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[[Image:1v0e.jpg|left|200px]]
[[Image:1v0e.jpg|left|200px]]
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{{Structure
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<!--
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|PDB= 1v0e |SIZE=350|CAPTION= <scene name='initialview01'>1v0e</scene>, resolution 1.90&Aring;
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The line below this paragraph, containing "STRUCTURE_1v0e", creates the "Structure Box" on the page.
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|SITE= <scene name='pdbsite=AC1:Po4+Binding+Site+For+Chain+D'>AC1</scene>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|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>
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or leave the SCENE parameter empty for the default display.
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|GENE=
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-->
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|DOMAIN=
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{{STRUCTURE_1v0e| PDB=1v0e | SCENE= }}
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|RELATEDENTRY=
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|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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}}
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'''ENDOSIALIDASE OF BACTERIOPHAGE K1F'''
'''ENDOSIALIDASE OF BACTERIOPHAGE K1F'''
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[[Category: Muehlenhoff, M.]]
[[Category: Muehlenhoff, M.]]
[[Category: Stummeyer, K.]]
[[Category: Stummeyer, K.]]
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[[Category: endosialidase]]
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[[Category: Endosialidase]]
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[[Category: glycosidase.]]
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[[Category: Glycosidase.]]
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[[Category: hydrolase]]
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[[Category: Hydrolase]]
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[[Category: polysialic acid degradation]]
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[[Category: Polysialic acid degradation]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 11:56:07 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:17:52 2008''
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Revision as of 08:56, 3 May 2008

Image:1v0e.jpg

Template:STRUCTURE 1v0e

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 Sat May 3 11:56:07 2008

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