2gr7
From Proteopedia
(New page: 200px<br /><applet load="2gr7" size="350" color="white" frame="true" align="right" spinBox="true" caption="2gr7, resolution 2.300Å" /> '''Hia 992-1098'''<br ...) |
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==Overview== | ==Overview== | ||
| - | Autotransporter proteins are defined by the ability to drive their own | + | Autotransporter proteins are defined by the ability to drive their own secretion across the bacterial outer membrane. The Hia autotransporter of Haemophilus influenzae belongs to the trimeric autotransporter subfamily and mediates bacterial adhesion to the respiratory epithelium. In this report, we present the crystal structure of the C-terminal end of Hia, corresponding to the entire Hia translocator domain and part of the passenger domain (residues 992-1098). This domain forms a beta-barrel with 12 transmembrane beta-strands, including four strands from each subunit. The beta-barrel has a central channel of 1.8 nm in diameter that is traversed by three N-terminal alpha-helices, one from each subunit. Mutagenesis studies demonstrate that the transmembrane portion of the three alpha-helices and the loop region between the alpha-helices and the neighboring beta-strands are essential for stability of the trimeric structure of the translocator domain, and that trimerization of the translocator domain is a prerequisite for translocator activity. Overall, this study provides important insights into the mechanism of translocation in trimeric autotransporters. |
==About this Structure== | ==About this Structure== | ||
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[[Category: trimeric autotransporter]] | [[Category: trimeric autotransporter]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:34:27 2008'' |
Revision as of 15:34, 21 February 2008
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Hia 992-1098
Overview
Autotransporter proteins are defined by the ability to drive their own secretion across the bacterial outer membrane. The Hia autotransporter of Haemophilus influenzae belongs to the trimeric autotransporter subfamily and mediates bacterial adhesion to the respiratory epithelium. In this report, we present the crystal structure of the C-terminal end of Hia, corresponding to the entire Hia translocator domain and part of the passenger domain (residues 992-1098). This domain forms a beta-barrel with 12 transmembrane beta-strands, including four strands from each subunit. The beta-barrel has a central channel of 1.8 nm in diameter that is traversed by three N-terminal alpha-helices, one from each subunit. Mutagenesis studies demonstrate that the transmembrane portion of the three alpha-helices and the loop region between the alpha-helices and the neighboring beta-strands are essential for stability of the trimeric structure of the translocator domain, and that trimerization of the translocator domain is a prerequisite for translocator activity. Overall, this study provides important insights into the mechanism of translocation in trimeric autotransporters.
About this Structure
2GR7 is a Single protein structure of sequence from Haemophilus influenzae with as ligand. Full crystallographic information is available from OCA.
Reference
Structure of the outer membrane translocator domain of the Haemophilus influenzae Hia trimeric autotransporter., Meng G, Surana NK, St Geme JW 3rd, Waksman G, EMBO J. 2006 Jun 7;25(11):2297-304. Epub 2006 May 11. PMID:16688217
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