1v0f

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
m (Protected "1v0f" [edit=sysop:move=sysop])
Current revision (07:50, 12 July 2023) (edit) (undo)
 
(7 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1v0f.png|left|200px]]
 
-
<!--
+
==Endosialidase of Bacteriophage K1F in complex with oligomeric alpha-2,8-sialic acid==
-
The line below this paragraph, containing "STRUCTURE_1v0f", creates the "Structure Box" on the page.
+
<StructureSection load='1v0f' size='340' side='right'caption='[[1v0f]], [[Resolution|resolution]] 2.55&Aring;' scene=''>
-
You may change the PDB parameter (which sets the PDB file loaded into the applet)
+
== Structural highlights ==
-
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+
<table><tr><td colspan='2'>[[1v0f]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_phage_K1F Escherichia phage K1F]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1V0F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1V0F FirstGlance]. <br>
-
or leave the SCENE parameter empty for the default display.
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.55&#8491;</td></tr>
-
-->
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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></td></tr>
-
{{STRUCTURE_1v0f| PDB=1v0f | SCENE= }}
+
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1v0f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1v0f OCA], [https://pdbe.org/1v0f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1v0f RCSB], [https://www.ebi.ac.uk/pdbsum/1v0f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1v0f ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/FIBER_BPK1F FIBER_BPK1F] Responsible for initial absorption of the phage to the host bacterium. Degrades the alpha-2,8-linked polysialic acid K1 capsule by cleaving within the polymer chain of polysialic acid.<ref>PMID:20096705</ref> <ref>PMID:3546309</ref> The C-terminal chaperone protein mediates homotrimerization and proper folding of the catalytic endo-N trimer.<ref>PMID:12556457</ref>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
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.
-
===ENDOSIALIDASE OF BACTERIOPHAGE K1F IN COMPLEX WITH OLIGOMERIC ALPHA-2,8-SIALIC ACID===
+
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<ref>PMID:15608653</ref>
-
 
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
<!--
+
</div>
-
The line below this paragraph, {{ABSTRACT_PUBMED_15608653}}, adds the Publication Abstract to the page
+
<div class="pdbe-citations 1v0f" style="background-color:#fffaf0;"></div>
-
(as it appears on PubMed at http://www.pubmed.gov), where 15608653 is the PubMed ID number.
+
== References ==
-
-->
+
<references/>
-
{{ABSTRACT_PUBMED_15608653}}
+
__TOC__
-
 
+
</StructureSection>
-
==About this Structure==
+
[[Category: Escherichia phage K1F]]
-
[[1v0f]] is a 6 chain structure with 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].
+
[[Category: Large Structures]]
-
 
+
[[Category: Dickmanns A]]
-
==Reference==
+
[[Category: Ficner R]]
-
<ref group="xtra">PMID:15608653</ref><ref group="xtra">PMID:12556457</ref><references group="xtra"/>
+
[[Category: Gerady-Schahn R]]
-
[[Category: Endo-alpha-sialidase]]
+
[[Category: Muehlenhoff M]]
-
[[Category: Enterobacteria phage k1f]]
+
[[Category: Stummeyer K]]
-
[[Category: Dickmanns, A.]]
+
-
[[Category: Ficner, R.]]
+
-
[[Category: Gerady-Schahn, R.]]
+
-
[[Category: Muehlenhoff, M.]]
+
-
[[Category: Stummeyer, K.]]
+
-
[[Category: Endosialidase]]
+
-
[[Category: Glycosidase.]]
+
-
[[Category: Hydrolase]]
+
-
[[Category: Polysialic acid degradation]]
+

Current revision

Endosialidase of Bacteriophage K1F in complex with oligomeric alpha-2,8-sialic acid

PDB ID 1v0f

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1v0f"
Personal tools