2odl
From Proteopedia
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Crystal structure of the HMW1 secretion domain from Haemophilus influenzae
Overview
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.
About this Structure
2ODL is a Single protein structure of sequence from Haemophilus influenzae. Full crystallographic information is available from OCA.
Reference
The structure of the Haemophilus influenzae HMW1 pro-piece reveals a structural domain essential for bacterial two-partner secretion., Yeo HJ, Yokoyama T, Walkiewicz K, Kim Y, Grass S, Geme JW 3rd, J Biol Chem. 2007 Oct 19;282(42):31076-84. Epub 2007 Aug 14. PMID:17699157
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