View source for 5fa1


==The structure of the beta-3-deoxy-D-manno-oct-2-ulosonic acid transferase domain of WbbB==
<StructureSection load='5fa1' size='340' side='right'caption='[[5fa1]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5fa1]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Raoultella_terrigena Raoultella terrigena]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FA1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5FA1 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=C5P:CYTIDINE-5-MONOPHOSPHATE'>C5P</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=5fa1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fa1 OCA], [https://pdbe.org/5fa1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5fa1 RCSB], [https://www.ebi.ac.uk/pdbsum/5fa1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5fa1 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q6U8B0_RAOTE Q6U8B0_RAOTE] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Kdo (3-deoxy-d-manno-oct-2-ulosonic acid) is an eight-carbon sugar mostly confined to Gram-negative bacteria. It is often involved in attaching surface polysaccharides to their lipid anchors. alpha-Kdo provides a bridge between lipid A and the core oligosaccharide in all bacterial LPSs, whereas an oligosaccharide of beta-Kdo residues links "group 2" capsular polysaccharides to (lyso)phosphatidylglycerol. beta-Kdo is also found in a small number of other bacterial polysaccharides. The structure and function of the prototypical cytidine monophosphate-Kdo-dependent alpha-Kdo glycosyltransferase from LPS assembly is well characterized. In contrast, the beta-Kdo counterparts were not identified as glycosyltransferase enzymes by bioinformatics tools and were not represented among the 98 currently recognized glycosyltransferase families in the Carbohydrate-Active Enzymes database. We report the crystallographic structure and function of a prototype beta-Kdo GT from WbbB, a modular protein participating in LPS O-antigen synthesis in Raoultella terrigena The beta-Kdo GT has dual Rossmann-fold motifs typical of GT-B enzymes, but extensive deletions, insertions, and rearrangements result in a unique architecture that makes it a prototype for a new GT family (GT99). The cytidine monophosphate-binding site in the C-terminal alpha/beta domain closely resembles the corresponding site in bacterial sialyltransferases, suggesting an evolutionary connection that is not immediately evident from the overall fold or sequence similarities.

Bacterial beta-Kdo glycosyltransferases represent a new glycosyltransferase family (GT99).,Ovchinnikova OG, Mallette E, Koizumi A, Lowary TL, Kimber MS, Whitfield C Proc Natl Acad Sci U S A. 2016 May 31;113(22):E3120-9. doi:, 10.1073/pnas.1603146113. Epub 2016 May 19. PMID:27199480<ref>PMID:27199480</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5fa1" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Raoultella terrigena]]
[[Category: Kimber MS]]
[[Category: Mallette E]]
[[Category: Ovchinnikova OG]]
[[Category: Whitfield C]]