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| | <StructureSection load='2odl' size='340' side='right'caption='[[2odl]], [[Resolution|resolution]] 1.92Å' scene=''> | | <StructureSection load='2odl' size='340' side='right'caption='[[2odl]], [[Resolution|resolution]] 1.92Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2odl]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacterium_influenzae"_lehmann_and_neumann_1896 "bacterium influenzae" lehmann and neumann 1896]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ODL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ODL FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2odl]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Haemophilus_influenzae Haemophilus influenzae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ODL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ODL FirstGlance]. <br> |
| - | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.92Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">hmw1A ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=727 "Bacterium influenzae" Lehmann and Neumann 1896])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> |
| | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2odl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2odl OCA], [https://pdbe.org/2odl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2odl RCSB], [https://www.ebi.ac.uk/pdbsum/2odl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2odl ProSAT]</span></td></tr> | | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2odl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2odl OCA], [https://pdbe.org/2odl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2odl RCSB], [https://www.ebi.ac.uk/pdbsum/2odl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2odl ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q48031_HAEIF Q48031_HAEIF] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacterium influenzae lehmann and neumann 1896]] | + | [[Category: Haemophilus influenzae]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Yeo, H J]] | + | [[Category: Yeo HJ]] |
| - | [[Category: Yokoyama, T]] | + | [[Category: Yokoyama T]] |
| - | [[Category: Beta helix]]
| + | |
| - | [[Category: Cell adhesion]]
| + | |
| - | [[Category: Hmw1]]
| + | |
| - | [[Category: Secretion domain]]
| + | |
| Structural highlights
Function
Q48031_HAEIF
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Yeo HJ, Yokoyama T, Walkiewicz K, Kim Y, Grass S, Geme JW 3rd. The structure of the Haemophilus influenzae HMW1 pro-piece reveals a structural domain essential for bacterial two-partner secretion. J Biol Chem. 2007 Oct 19;282(42):31076-84. Epub 2007 Aug 14. PMID:17699157 doi:10.1074/jbc.M705750200
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