4UZG

Crystal structure of group B streptococcus pilus 2b backbone protein SAK_1440

4UZG の概要

• エントリーDOI: 10.2210/pdb4uzg/pdb
• 分子名称: SURFACE PROTEIN SPB1, 1,2-ETHANEDIOL, CALCIUM ION, ... (4 entities in total)
• 機能のキーワード: structural protein, pili, sortases, isopeptide bond
• 由来する生物種: STREPTOCOCCUS AGALACTIAE A909
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 31690.74

構造登録者

Malito, E.,Cozzi, R.,Bottomley, M.J. (登録日: 2014-09-05, 公開日: 2015-05-13, 最終更新日: 2024-11-06)

主引用文献

Cozzi, R.,Malito, E.,Lazzarin, M.,Nuccitelli, A.,Castagnetti, A.,Bottomley, M.J.,Margarit, I.,Maione, D.,Rinaudo, C.D.
Structure and assembly of group B streptococcus pilus 2b backbone protein.
PLoS ONE, 10:e0125875-e0125875, 2015

PubMed Abstract: Group B Streptococcus (GBS) is a major cause of invasive disease in infants. Like other Gram-positive bacteria, GBS uses a sortase C-catalyzed transpeptidation mechanism to generate cell surface pili from backbone and ancillary pilin precursor substrates. The three pilus types identified in GBS contain structural subunits that are highly immunogenic and are promising candidates for the development of a broadly-protective vaccine. Here we report the X-ray crystal structure of the backbone protein of pilus 2b (BP-2b) at 1.06Å resolution. The structure reveals a classical IgG-like fold typical of the pilin subunits of other Gram-positive bacteria. The crystallized portion of the protein (residues 185-468) encompasses domains D2 and D3 that together confer high stability to the protein due to the presence of an internal isopeptide bond within each domain. The D2+D3 region, lacking the N-terminal D1 domain, was as potent as the entire protein in conferring protection against GBS challenge in a well-established mouse model. By site-directed mutagenesis and complementation studies in GBS knock-out strains we identified the residues and motives essential for assembly of the BP-2b monomers into high-molecular weight complexes, thus providing new insights into pilus 2b polymerization.

PubMed: 25942637
DOI: 10.1371/journal.pone.0125875

実験手法

X-RAY DIFFRACTION (1.06 Å)