2odl: Difference between revisions

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[[Image:2odl.jpg|left|200px]]
{{Seed}}
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{{STRUCTURE_2odl|  PDB=2odl  |  SCENE=  }}  
{{STRUCTURE_2odl|  PDB=2odl  |  SCENE=  }}  


'''Crystal structure of the HMW1 secretion domain from Haemophilus influenzae'''
===Crystal structure of the HMW1 secretion domain from Haemophilus influenzae===




==Overview==
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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.
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{{ABSTRACT_PUBMED_17699157}}


==About this Structure==
==About this Structure==
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[[Category: Hmw1]]
[[Category: Hmw1]]
[[Category: Secretion domain]]
[[Category: Secretion domain]]
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