1v0f
From Proteopedia
| Line 5: | Line 5: | ||
==Overview== | ==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, ... | + | 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== | ==About this Structure== | ||
| - | 1V0F is a | + | 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 SLB and PO4 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] Structure known Active Site: AC1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1V0F OCA]. |
==Reference== | ==Reference== | ||
| Line 27: | Line 27: | ||
[[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 Mon Nov 5 14:45:50 2007'' |
Revision as of 12:40, 5 November 2007
|
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 with SLB and PO4 as ligands. Active as Endo-alpha-sialidase, with EC number 3.2.1.129 Structure known Active Site: AC1. 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 Mon Nov 5 14:45:50 2007
