5WC6

Structure of a bacterial polysialyltransferase at 2.2 Angstrom resolution

5WC6 の概要

• エントリーDOI: 10.2210/pdb5wc6/pdb
• 分子名称: SiaD, SULFATE ION (3 entities in total)
• 機能のキーワード: polysialyltransferase, gt-b, membrane protein
• 由来する生物種: Mannheimia haemolytica
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 90802.23

構造登録者

Worrall, L.J.,Lizak, C.,Strynadka, N.C.J. (登録日: 2017-06-29, 公開日: 2017-08-02, 最終更新日: 2019-11-20)

主引用文献

Lizak, C.,Worrall, L.J.,Baumann, L.,Pfleiderer, M.M.,Volkers, G.,Sun, T.,Sim, L.,Wakarchuk, W.,Withers, S.G.,Strynadka, N.C.J.
X-ray crystallographic structure of a bacterial polysialyltransferase provides insight into the biosynthesis of capsular polysialic acid.
Sci Rep, 7:5842-5842, 2017

PubMed Abstract: 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.

PubMed: 28724897
DOI: 10.1038/s41598-017-05627-z

実験手法

X-RAY DIFFRACTION (2.2 Å)