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New page: ==Structure of a bacterial polysialyltransferase in complex with CDP== <StructureSection load='5wcn' size='340' side='right' caption='5wcn, resolution 3.00Å' scen...
 
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==Structure of a bacterial polysialyltransferase in complex with CDP==
==Structure of a bacterial polysialyltransferase in complex with CDP==
<StructureSection load='5wcn' size='340' side='right' caption='[[5wcn]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
<StructureSection load='5wcn' size='340' side='right'caption='[[5wcn]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[5wcn]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5WCN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5WCN FirstGlance]. <br>
<table><tr><td colspan='2'>[[5wcn]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mannheimia_haemolytica Mannheimia haemolytica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5WCN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5WCN FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CDP:CYTIDINE-5-DIPHOSPHATE'>CDP</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5wcn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5wcn OCA], [http://pdbe.org/5wcn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5wcn RCSB], [http://www.ebi.ac.uk/pdbsum/5wcn PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5wcn ProSAT]</span></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CDP:CYTIDINE-5-DIPHOSPHATE'>CDP</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5wcn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5wcn OCA], [https://pdbe.org/5wcn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5wcn RCSB], [https://www.ebi.ac.uk/pdbsum/5wcn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5wcn ProSAT]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
== Function ==
== Publication Abstract from PubMed ==
[https://www.uniprot.org/uniprot/G4RIN4_MANHA G4RIN4_MANHA]
Polysialic acid (polySia) is a homopolymeric saccharide that is associated with some neuroinvasive pathogens and is found on selective cell types in their eukaryotic host. The presence of a polySia capsule on these bacterial pathogens helps with resistance to phagocytosis, cationic microbial peptides and bactericidal antibody production. The biosynthesis of bacterial polySia is catalysed by a single polysialyltransferase (PST) transferring sialic acid from a nucleotide-activated donor to a lipid-linked acceptor oligosaccharide. Here we present the X-ray structure of the bacterial PST from Mannheimia haemolytica serotype A2, thereby defining the architecture of this class of enzymes representing the GT38 family. The structure reveals a prominent electropositive groove between the two Rossmann-like domains forming the GT-B fold that is suitable for binding of polySia chain products. Complex structures of PST with a sugar donor analogue and an acceptor mimetic combined with kinetic studies of PST active site mutants provide insight into the principles of substrate binding and catalysis. Our results are the basis for a molecular understanding of polySia biosynthesis in bacteria and might assist the production of polysialylated therapeutic reagents and the development of novel antibiotics.
 
X-ray crystallographic structure of a bacterial polysialyltransferase provides insight into the biosynthesis of capsular polysialic acid.,Lizak C, Worrall LJ, Baumann L, Pfleiderer MM, Volkers G, Sun T, Sim L, Wakarchuk W, Withers SG, Strynadka NCJ Sci Rep. 2017 Jul 19;7(1):5842. doi: 10.1038/s41598-017-05627-z. PMID:28724897<ref>PMID:28724897</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5wcn" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Lizak, C]]
[[Category: Large Structures]]
[[Category: Strynadka, N C.J]]
[[Category: Mannheimia haemolytica]]
[[Category: Worrall, L J]]
[[Category: Lizak C]]
[[Category: Gt-b]]
[[Category: Strynadka NCJ]]
[[Category: Membrane protein]]
[[Category: Worrall LJ]]
[[Category: Polysialyltransferase]]

Latest revision as of 14:15, 13 March 2024

Structure of a bacterial polysialyltransferase in complex with CDP

5wcn, resolution 3.00Å

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