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| | <StructureSection load='4c47' size='340' side='right'caption='[[4c47]], [[Resolution|resolution]] 2.45Å' scene=''> | | <StructureSection load='4c47' size='340' side='right'caption='[[4c47]], [[Resolution|resolution]] 2.45Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4c47]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Salty Salty]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C47 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4C47 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4c47]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Salmonella_enterica_subsp._enterica_serovar_Typhimurium_str._LT2 Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C47 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4C47 FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4c46|4c46]]</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]] 2.448Å</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4c47 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c47 OCA], [http://pdbe.org/4c47 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4c47 RCSB], [http://www.ebi.ac.uk/pdbsum/4c47 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4c47 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=4c47 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c47 OCA], [https://pdbe.org/4c47 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4c47 RCSB], [https://www.ebi.ac.uk/pdbsum/4c47 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4c47 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/SADB_SALTY SADB_SALTY] Required for proper surface expression of the autotransporter adhesin SadA. Could be directly involved in the biogenesis of functionally active SadA.<ref>PMID:24369174</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Salty]] | + | [[Category: Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]] |
| - | [[Category: Grin, I]] | + | [[Category: Grin I]] |
| - | [[Category: Hartmann, M D]] | + | [[Category: Hartmann MD]] |
| - | [[Category: Linke, D]] | + | [[Category: Linke D]] |
| - | [[Category: Autotransport]]
| + | |
| - | [[Category: Bacterial adhesion]]
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| - | [[Category: Cell adhesion]]
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| - | [[Category: Membrane insertion]]
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| - | [[Category: Membrane trafficking]]
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| - | [[Category: Polar core residue]]
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| Structural highlights
Function
SADB_SALTY Required for proper surface expression of the autotransporter adhesin SadA. Could be directly involved in the biogenesis of functionally active SadA.[1]
Publication Abstract from PubMed
Trimeric Autotransporter Adhesins (TAAs) are important virulence factors of many gram-negative bacterial pathogens. TAAs form fibrous, adhesive structures on the bacterial cell surface. Their N-terminal, extracellular domains are exported through a C-terminal membrane pore; the insertion of the pore domain into the bacterial outer membrane follows the rules of beta-barrel transmembrane protein biogenesis and is dependent on the essential Bam complex. We have recently described the full fiber structure of SadA, a TAA of unknown function in Salmonella and other enterobacteria. In this work, we describe the structure and function of SadB, a small inner membrane lipoprotein. The sadB gene is located in an operon with sadA; orthologous operons are only found in enterobacteria, while other TAAs are not typically associated with lipoproteins. Strikingly, SadB is also a trimer, and its co-expression with SadA has a direct influence on SadA structural integrity. This is the first report of a specific export factor of a TAA, suggesting that at least in some cases, TAA autotransport is assisted by additional periplasmic proteins.
A Trimeric Lipoprotein assists in Trimeric Autotransporter Biogenesis in Enterobacteria.,Grin I, Hartmann MD, Sauer G, Hernandez Alvarez B, Schutz M, Madlung J, Macek B, Felipe-Lopez A, Hensel M, Lupas A, Linke D J Biol Chem. 2013 Dec 25. PMID:24369174[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Grin I, Hartmann MD, Sauer G, Hernandez Alvarez B, Schutz M, Madlung J, Macek B, Felipe-Lopez A, Hensel M, Lupas A, Linke D. A Trimeric Lipoprotein assists in Trimeric Autotransporter Biogenesis in Enterobacteria. J Biol Chem. 2013 Dec 25. PMID:24369174 doi:http://dx.doi.org/10.1074/jbc.M113.513275
- ↑ Grin I, Hartmann MD, Sauer G, Hernandez Alvarez B, Schutz M, Madlung J, Macek B, Felipe-Lopez A, Hensel M, Lupas A, Linke D. A Trimeric Lipoprotein assists in Trimeric Autotransporter Biogenesis in Enterobacteria. J Biol Chem. 2013 Dec 25. PMID:24369174 doi:http://dx.doi.org/10.1074/jbc.M113.513275
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