1v0f

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[[Image:1v0f.jpg|left|200px]]<br /><applet load="1v0f" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1v0f.jpg|left|200px]]
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caption="1v0f, resolution 2.55&Aring;" />
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'''ENDOSIALIDASE OF BACTERIOPHAGE K1F IN COMPLEX WITH OLIGOMERIC ALPHA-2,8-SIALIC ACID'''<br />
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{{Structure
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|PDB= 1v0f |SIZE=350|CAPTION= <scene name='initialview01'>1v0f</scene>, resolution 2.55&Aring;
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|SITE= <scene name='pdbsite=AC1:Po4+Binding+Site+For+Chain+D'>AC1</scene>
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|LIGAND= <scene name='pdbligand=SLB:5-N-ACETYL-BETA-D-NEURAMINIC+ACID'>SLB</scene> and <scene name='pdbligand=PO4:PHOSPHATE ION'>PO4</scene>
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|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]
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|GENE=
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}}
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'''ENDOSIALIDASE OF BACTERIOPHAGE K1F IN COMPLEX WITH OLIGOMERIC ALPHA-2,8-SIALIC ACID'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1V0F is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Enterobacteria_phage_k1f Enterobacteria phage k1f] with <scene name='pdbligand=SLB:'>SLB</scene> and <scene name='pdbligand=PO4:'>PO4</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. 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://oca.weizmann.ac.il/oca-bin/ocashort?id=1V0F OCA].
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1V0F 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=1V0F OCA].
==Reference==
==Reference==
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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://ispc.weizmann.ac.il//pmbin/getpm?pmid=15608653 15608653]
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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: Enterobacteria phage k1f]]
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[[Category: polysialic acid degradation]]
[[Category: polysialic acid degradation]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:30:21 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:39:18 2008''

Revision as of 12:39, 20 March 2008


PDB ID 1v0f

Drag the structure with the mouse to rotate
, resolution 2.55Å
Sites:
Ligands: and
Activity: Endo-alpha-sialidase, with EC number 3.2.1.129
Coordinates: save as pdb, mmCIF, xml



ENDOSIALIDASE OF BACTERIOPHAGE K1F IN COMPLEX WITH OLIGOMERIC ALPHA-2,8-SIALIC ACID


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

1V0F 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

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