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5CFV

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

Summary for 5CFV
Entry DOI10.2210/pdb5cfv/pdb
Related3SOK 4XA2
Related PRD IDPRD_900001
DescriptorMaltose-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)
Functional Keywordsadhesion, extracellular appendage, fimbriae, cell adhesion
Biological sourceEscherichia coli
More
Total number of polymer chains1
Total formula weight54265.45
Authors
Piepenbrink, K.H.,Sundberg, E.J. (deposition date: 2015-07-08, release date: 2016-07-13, Last modification date: 2024-10-23)
Primary citationPiepenbrink, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.8 Å)
Structure validation

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