6BEA

Crystal structure of the autotransporter UpaB from E. coli strain CFT073

Summary for 6BEA

• Entry DOI: 10.2210/pdb6bea/pdb
• Related: 4KH3
• Descriptor: Autotransporter protein UpaB, GLYCEROL, HEXAETHYLENE GLYCOL, ... (8 entities in total)
• Functional Keywords: autotransporter protein, bacterial adhesin, virulence factor, fibronectin, glycosaminoglycan, protein binding
• Biological source: Escherichia coli O6:H1
• Total number of polymer chains: 1
• Total formula weight: 48668.76

Authors

Paxman, J.J.,Heras, B. (deposition date: 2017-10-25, release date: 2019-04-10, Last modification date: 2024-03-13)

Primary citation

Paxman, J.J.,Lo, A.W.,Sullivan, M.J.,Panjikar, S.,Kuiper, M.,Whitten, A.E.,Wang, G.,Luan, C.H.,Moriel, D.G.,Tan, L.,Peters, K.M.,Phan, M.D.,Gee, C.L.,Ulett, G.C.,Schembri, M.A.,Heras, B.
Unique structural features of a bacterial autotransporter adhesin suggest mechanisms for interaction with host macromolecules.
Nat Commun, 10:1967-1967, 2019

PubMed Abstract: Autotransporters are the largest family of outer membrane and secreted proteins in Gram-negative bacteria. Most autotransporters are localised to the bacterial surface where they promote colonisation of host epithelial surfaces. Here we present the crystal structure of UpaB, an autotransporter that is known to contribute to uropathogenic E. coli (UPEC) colonisation of the urinary tract. We provide evidence that UpaB can interact with glycosaminoglycans and host fibronectin. Unique modifications to its core β-helical structure create a groove on one side of the protein for interaction with glycosaminoglycans, while the opposite face can bind fibronectin. Our findings reveal far greater diversity in the autotransporter β-helix than previously thought, and suggest that this domain can interact with host macromolecules. The relevance of these interactions during infection remains unclear.

PubMed: 31036849
DOI: 10.1038/s41467-019-09814-6

Experimental method

X-RAY DIFFRACTION (1.97 Å)