2odl

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[[Image:2odl.jpg|left|200px]]
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{{Structure
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|PDB= 2odl |SIZE=350|CAPTION= <scene name='initialview01'>2odl</scene>, resolution 1.92&Aring;
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The line below this paragraph, containing "STRUCTURE_2odl", creates the "Structure Box" on the page.
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|GENE= hmw1A ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=727 Haemophilus influenzae])
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{{STRUCTURE_2odl| PDB=2odl | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2odl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2odl OCA], [http://www.ebi.ac.uk/pdbsum/2odl PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2odl RCSB]</span>
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'''Crystal structure of the HMW1 secretion domain from Haemophilus influenzae'''
'''Crystal structure of the HMW1 secretion domain from Haemophilus influenzae'''
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[[Category: Yeo, H J.]]
[[Category: Yeo, H J.]]
[[Category: Yokoyama, T.]]
[[Category: Yokoyama, T.]]
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[[Category: beta helix]]
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[[Category: Beta helix]]
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[[Category: cell adhesion]]
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[[Category: Cell adhesion]]
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[[Category: hmw1]]
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[[Category: Hmw1]]
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[[Category: secretion domain]]
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[[Category: Secretion domain]]
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Revision as of 07:40, 4 May 2008

Template:STRUCTURE 2odl

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 Page seeded by OCA on Sun May 4 10:40:55 2008

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