1v0f
From Proteopedia
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|PDB= 1v0f |SIZE=350|CAPTION= <scene name='initialview01'>1v0f</scene>, resolution 2.55Å | |PDB= 1v0f |SIZE=350|CAPTION= <scene name='initialview01'>1v0f</scene>, resolution 2.55Å | ||
|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= | + | |LIGAND= <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=SIA:O-SIALIC+ACID'>SIA</scene>, <scene name='pdbligand=SLB:5-N-ACETYL-BETA-D-NEURAMINIC+ACID'>SLB</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=1v0f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1v0f OCA], [http://www.ebi.ac.uk/pdbsum/1v0f PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1v0f RCSB]</span> | ||
}} | }} | ||
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[[Category: Muehlenhoff, M.]] | [[Category: Muehlenhoff, M.]] | ||
[[Category: Stummeyer, K.]] | [[Category: Stummeyer, K.]] | ||
| - | [[Category: PO4]] | ||
| - | [[Category: SLB]] | ||
[[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 2.55Å | |||||||
|---|---|---|---|---|---|---|---|
| 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 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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