6EFA

GspB Siglec + Unique domains

6EFA の概要

• エントリーDOI: 10.2210/pdb6efa/pdb
• 関連するPDBエントリー: 5IUC 6EF7 6EF9 6EFB 6EFC 6EFD 6EFF 6EFI
• 分子名称: Platelet binding protein GspB, CALCIUM ION (3 entities in total)
• 機能のキーワード: lectin, sugar binding protein
• 由来する生物種: Streptococcus gordonii
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 22817.32

構造登録者

Iverson, T.M. (登録日: 2018-08-16, 公開日: 2020-02-19, 最終更新日: 2024-05-22)

主引用文献

Bensing, B.A.,Stubbs, H.E.,Agarwal, R.,Yamakawa, I.,Luong, K.,Solakyildirim, K.,Yu, H.,Hadadianpour, A.,Castro, M.A.,Fialkowski, K.P.,Morrison, K.M.,Wawrzak, Z.,Chen, X.,Lebrilla, C.B.,Baudry, J.,Smith, J.C.,Sullam, P.M.,Iverson, T.M.
Origins of glycan selectivity in streptococcal Siglec-like adhesins suggest mechanisms of receptor adaptation.
Nat Commun, 13:2753-2753, 2022

PubMed Abstract: Bacterial binding to host receptors underlies both commensalism and pathogenesis. Many streptococci adhere to protein-attached carbohydrates expressed on cell surfaces using Siglec-like binding regions (SLBRs). The precise glycan repertoire recognized may dictate whether the organism is a strict commensal versus a pathogen. However, it is currently not clear what drives receptor selectivity. Here, we use five representative SLBRs and identify regions of the receptor binding site that are hypervariable in sequence and structure. We show that these regions control the identity of the preferred carbohydrate ligand using chimeragenesis and single amino acid substitutions. We further evaluate how the identity of the preferred ligand affects the interaction with glycoprotein receptors in human saliva and plasma samples. As point mutations can change the preferred human receptor, these studies suggest how streptococci may adapt to changes in the environmental glycan repertoire.

PubMed: 35585145
DOI: 10.1038/s41467-022-30509-y

実験手法

X-RAY DIFFRACTION (1.6 Å)