3EMI
Crystal structure of Hia 307-422 non-adhesive domain
Summary for 3EMI
Entry DOI | 10.2210/pdb3emi/pdb |
Related | 1s7m 2gr7 2gr8 3EMF 3EMO |
Descriptor | Hia (Adhesin) (2 entities in total) |
Functional Keywords | non-adhesive domain, hia adhesin, trimeric autotransporter, haemophilus influenzae, cell adhesion |
Biological source | Haemophilus influenzae |
Total number of polymer chains | 1 |
Total formula weight | 12047.25 |
Authors | Meng, G.,Waksman, G. (deposition date: 2008-09-24, release date: 2008-11-04, Last modification date: 2024-05-29) |
Primary citation | Meng, 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: 18948113DOI: 10.1016/j.jmb.2008.09.085 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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