5fa1 | pdb_00005fa1

The structure of the beta-3-deoxy-D-manno-oct-2-ulosonic acid transferase domain of WbbB

spinqualitylabelsall models 5fa1, resolution 2.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5fa1 is a 2 chain structure with sequence from Raoultella terrigena. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.1Å Ligands: C5P Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q6U8B0_RAOTE 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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