5D55

Crystal structure of the E. coli Hda pilus minor tip subunit, HdaB

Summary for 5D55

• Entry DOI: 10.2210/pdb5d55/pdb
• Descriptor: HdaB,HdaA (Adhesin), HUS-associated diffuse adherence, CITRATE ANION, IODIDE ION, ... (4 entities in total)
• Functional Keywords: biofilm, cell adhesion, chaperone-usher, hda, pilus
• Biological source: Escherichia coli; More
• Total number of polymer chains: 2
• Total formula weight: 35671.54

Authors

Lee, W.-C.,Garnett, J.A.,Matthews, S.J. (deposition date: 2015-08-10, release date: 2016-08-10, Last modification date: 2024-11-20)

Primary citation

Lee, W.C.,Matthews, S.,Garnett, J.A.
Crystal structure and analysis of HdaB: The enteroaggregative Escherichia coli AAF/IV pilus tip protein.
Protein Sci., 25:1898-1905, 2016

PubMed Abstract: Enteroaggregative Escherichia coli is the primary cause of pediatric diarrhea in developing countries. They utilize aggregative adherence fimbriae (AAFs) to promote initial adherence to the host intestinal mucosa, promote the formation of biofilms, and mediate host invasion. Five AAFs have been identified to date and AAF/IV is amongst the most prevalent found in clinical isolates. Here we present the X-ray crystal structure of the AAF/IV tip protein HdaB at 2.0 Å resolution. It shares high structural homology with members of the Afa/Dr superfamily of fimbriae, which are involved in host invasion. We highlight surface exposed residues that share sequence homology and propose that these may function in invasion and also non-conserved regions that could mediate HdaB specific adhesive functions.

PubMed: 27400770
DOI: 10.1002/pro.2982

Experimental method

X-RAY DIFFRACTION (2 Å)