5cfv
From Proteopedia
Fusion of Maltose-binding Protein and PilA from Acinetobacter nosocomialis M2
Structural highlights
FunctionMALE_ECOLI Involved in the high-affinity maltose membrane transport system MalEFGK. Initial receptor for the active transport of and chemotaxis toward maltooligosaccharides. Publication Abstract from PubMedAcinetobacter 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, a bacterial extracellular appendage 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 which has resulted in three distinct classes of type IVa pilins, each found in multiple species. Structural diversity in the type IV pili of multidrug-resistant Acinetobacter.,Piepenbrink KJ, Lillehoj EP, Harding CM, Labonte JW, Zuo X, Rapp CA, Munson RS Jr, Goldblum SE, Feldman MF, Gray JJ, Sundberg EJ J Biol Chem. 2016 Sep 15. pii: jbc.M116.751099. PMID:27634041[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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