2ODL

Crystal structure of the HMW1 secretion domain from Haemophilus influenzae

2ODL の概要

• エントリーDOI: 10.2210/pdb2odl/pdb
• 分子名称: Adhesin (2 entities in total)
• 機能のキーワード: hmw1, secretion domain, beta helix, cell adhesion
• 由来する生物種: Haemophilus influenzae
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 39362.39

構造登録者

Yokoyama, T.,Yeo, H.J. (登録日: 2006-12-22, 公開日: 2007-08-21, 最終更新日: 2024-11-20)

主引用文献

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

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: 17699157
DOI: 10.1074/jbc.M705750200

実験手法

X-RAY DIFFRACTION (1.92 Å)