5CFV

Fusion of Maltose-binding Protein and PilA from Acinetobacter nosocomialis M2

5CFV の概要

• エントリーDOI: 10.2210/pdb5cfv/pdb
• 関連するPDBエントリー: 3SOK 4XA2
• 関連するBIRD辞書のPRD_ID: PRD_900001
• 分子名称: Maltose-binding periplasmic protein,Maltose-binding periplasmic protein,PilA fusion protein, alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose, (4S)-2-METHYL-2,4-PENTANEDIOL, ... (6 entities in total)
• 機能のキーワード: adhesion, extracellular appendage, fimbriae, cell adhesion
• 由来する生物種: Escherichia coli; 詳細
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 54265.45

構造登録者

Piepenbrink, K.H.,Sundberg, E.J. (登録日: 2015-07-08, 公開日: 2016-07-13, 最終更新日: 2024-10-23)

主引用文献

Piepenbrink, K.H.,Lillehoj, E.,Harding, C.M.,Labonte, J.W.,Zuo, X.,Rapp, C.A.,Munson, R.S.,Goldblum, S.E.,Feldman, M.F.,Gray, J.J.,Sundberg, E.J.
Structural Diversity in the Type IV Pili of Multidrug-resistant Acinetobacter.
J.Biol.Chem., 291:22924-22935, 2016

PubMed Abstract: Acinetobacter baumannii is a Gram-negative coccobacillus found primarily in hospital settings that has recently emerged as a source of hospital-acquired infections. A. baumannii expresses a variety of virulence factors, including type IV pili, bacterial extracellular appendages often essential for attachment to host cells. Here, we report the high resolution structures of the major pilin subunit, PilA, from three Acinetobacter strains, demonstrating that A. baumannii subsets produce morphologically distinct type IV pilin glycoproteins. We examine the consequences of this heterogeneity for protein folding and assembly as well as host-cell adhesion by Acinetobacter Comparisons of genomic and structural data with pilin proteins from other species of soil gammaproteobacteria suggest that these structural differences stem from evolutionary pressure that has resulted in three distinct classes of type IVa pilins, each found in multiple species.

PubMed: 27634041
DOI: 10.1074/jbc.M116.751099

実験手法

X-RAY DIFFRACTION (1.8 Å)