2ODL
Crystal structure of the HMW1 secretion domain from Haemophilus influenzae
Summary for 2ODL
| Entry DOI | 10.2210/pdb2odl/pdb |
| Descriptor | Adhesin (2 entities in total) |
| Functional Keywords | hmw1, secretion domain, beta helix, cell adhesion |
| Biological source | Haemophilus influenzae |
| Total number of polymer chains | 1 |
| Total formula weight | 39362.39 |
| Authors | Yokoyama, T.,Yeo, H.J. (deposition date: 2006-12-22, release date: 2007-08-21, Last modification date: 2024-11-20) |
| Primary citation | Yeo, H.J.,Yokoyama, T.,Walkiewicz, K.,Kim, Y.,Grass, S.,Geme, J.W. The structure of the Haemophilus influenzae HMW1 pro-piece reveals a structural domain essential for bacterial two-partner secretion. J.Biol.Chem., 282:31076-31084, 2007 Cited by PubMed Abstract: In pathogenic Gram-negative bacteria, many virulence factors are secreted via the two-partner secretion pathway, which consists of an exoprotein called TpsA and a cognate outer membrane translocator called TpsB. The HMW1 and HMW2 adhesins are major virulence factors in nontypeable Haemophilus influenzae and are prototype two-partner secretion pathway exoproteins. A key step in the delivery of HMW1 and HMW2 to the bacterial surface involves targeting to the HMW1B and HMW2B outer membrane translocators by an N-terminal region called the secretion domain. Here we present the crystal structure at 1.92 A of the HMW1 pro-piece (HMW1-PP), a region that contains the HMW1 secretion domain and is cleaved and released during HMW1 secretion. Structural analysis of HMW1-PP revealed a right-handed beta-helix fold containing 12 complete parallel coils and one large extra-helical domain. Comparison of HMW1-PP and the Bordetella pertussis FHA secretion domain (Fha30) reveals limited amino acid homology but shared structural features, suggesting that diverse TpsA proteins have a common structural domain required for targeting to cognate TpsB proteins. Further comparison of HMW1-PP and Fha30 structures may provide insights into the keen specificity of TpsA-TpsB interactions. PubMed: 17699157DOI: 10.1074/jbc.M705750200 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.92 Å) |
Structure validation
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