3FAW

Crystal Structure of the Group B Streptococcus Pullulanase SAP

3FAW の概要

• エントリーDOI: 10.2210/pdb3faw/pdb
• 関連するPDBエントリー: 3FAX
• 分子名称: Reticulocyte binding protein, CALCIUM ION, CHLORIDE ION, ... (4 entities in total)
• 機能のキーワード: tim barrel, beta barrel, hydrolase, cell wall, peptidoglycan-anchor, secreted
• 由来する生物種: Streptococcus agalactiae COH1
• 細胞内の位置: Secreted, cell wall; Peptidoglycan-anchor (By similarity): Q3DB05
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 98895.15

構造登録者

Gourlay, L.J. (登録日: 2008-11-18, 公開日: 2009-04-14, 最終更新日: 2023-11-01)

主引用文献

Gourlay, L.J.,Santi, I.,Pezzicoli, A.,Grandi, G.,Soriani, M.,Bolognesi, M.
Group B Streptococcus pullulanase crystal structures in the context of a novel strategy for vaccine development
J.Bacteriol., 191:3544-3552, 2009

PubMed Abstract: The group B streptococcus type I pullulanase (SAP) is a class 13 glycoside hydrolase that is anchored to the bacterial cell surface via a conserved C-terminal anchoring motif and involved in alpha-glucan degradation. Recent in vitro functional studies have shown that SAP is immunogenic in humans and that anti-SAP sera derived from immunized animals impair both group A and group B streptococcus pullulanase activities, suggesting that in vivo immunization with this antigen could prevent streptococcal colonization. To further investigate the putative role of SAP in bacterial pathogenesis, we carried out functional studies and found that recombinant SAP binds to human cervical epithelial cells. Furthermore, with a view of using SAP as a vaccine candidate, we present high-resolution crystal structure analyses of an N-terminally truncated form of SAP lacking the carbohydrate binding module but containing the catalytic domain and displaying glycosidase hydrolase activity, both in its apo form and in complex with maltotetraose, at resolutions of 2.1 and 2.4 A, respectively.

PubMed: 19329633
DOI: 10.1128/JB.01755-08

実験手法

X-RAY DIFFRACTION (2.1 Å)