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3EMF

Crystal structure of Haemophilus influenzae HiaBD2

Summary for 3EMF
Entry DOI10.2210/pdb3emf/pdb
Related1s7m 2gr7 2gr8 3EMI 3EMO
DescriptorHia (Adhesin) (2 entities in total)
Functional Keywordshia, adhesin, binding domain, autotransporter, trimeric, cell adhesion
Biological sourceHaemophilus influenzae
Total number of polymer chains3
Total formula weight37790.68
Authors
Meng, G.,Waksman, G. (deposition date: 2008-09-24, release date: 2008-11-04, Last modification date: 2025-05-28)
Primary citationMeng, G.,St Geme, J.W.,Waksman, G.
Repetitive Architecture of the Haemophilus influenzae Hia Trimeric Autotransporter
J.Mol.Biol., 384:824-836, 2008
Cited by
PubMed Abstract: The Hia autotransporter of Haemophilus influenzae belongs to the trimeric autotransporter subfamily and mediates bacterial adherence to the respiratory epithelium. In this report, we show that the structure of Hia is characterized by a modular architecture containing repeats of structurally distinct domains. Comparison of the structures of HiaBD1 and HiaBD2 adhesive repeats and a nonadhesive repeat (a novel fold) shed light on the structural determinants of Hia adhesive function. Examination of the structure of an extended version of the Hia translocator domain revealed the structural transition between the C-terminal translocator domain and the N-terminal passenger domain, highlighting a highly intertwined domain that is ubiquitous among trimeric autotransporters. Overall, this study provides important insights into the mechanism of Hia adhesive activity and the overall structure of trimeric autotransporters.
PubMed: 18948113
DOI: 10.1016/j.jmb.2008.09.085
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2 Å)
Structure validation

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