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| | ==The structure of TamB963-1138 from Escherichia coli reveals a novel hydrophobic Beta-taco fold== | | ==The structure of TamB963-1138 from Escherichia coli reveals a novel hydrophobic Beta-taco fold== |
| - | <StructureSection load='5vtg' size='340' side='right' caption='[[5vtg]], [[Resolution|resolution]] 1.86Å' scene=''> | + | <StructureSection load='5vtg' size='340' side='right'caption='[[5vtg]], [[Resolution|resolution]] 1.86Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5vtg]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5VTG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5VTG FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5vtg]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5VTG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5VTG FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">tamB, ytfN, ytfO, b4221, JW4180 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</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]] 1.859Å</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=5vtg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5vtg OCA], [http://pdbe.org/5vtg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5vtg RCSB], [http://www.ebi.ac.uk/pdbsum/5vtg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5vtg 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=5vtg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5vtg OCA], [https://pdbe.org/5vtg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5vtg RCSB], [https://www.ebi.ac.uk/pdbsum/5vtg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5vtg ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/TAMB_ECOLI TAMB_ECOLI]] Part of the translocation and assembly module (TAM) autotransporter assembly complex, which functions in translocation of autotransporters across the outer membrane (PubMed:22466966). In reconstituted TAM this subunit (Ag43, AC P39180) is not necessary for substrate penetration in the outer membrane. Substrate binding to TamA moves its POTRA domains about 30 Angstroms into the periplasm, which would deform either the outer membrane or TamB and may provide force to reset TAM (PubMed:25341963).<ref>PMID:22466966</ref> <ref>PMID:25341963</ref> | + | [https://www.uniprot.org/uniprot/TAMB_ECOLI TAMB_ECOLI] Part of the translocation and assembly module (TAM) autotransporter assembly complex, which functions in translocation of autotransporters across the outer membrane (PubMed:22466966). In reconstituted TAM this subunit (Ag43, AC P39180) is not necessary for substrate penetration in the outer membrane. Substrate binding to TamA moves its POTRA domains about 30 Angstroms into the periplasm, which would deform either the outer membrane or TamB and may provide force to reset TAM (PubMed:25341963).<ref>PMID:22466966</ref> <ref>PMID:25341963</ref> |
| - | <div style="background-color:#fffaf0;">
| + | |
| - | == Publication Abstract from PubMed ==
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| - | The translocation and assembly module (TAM) plays a role in the transport and insertion of proteins into the bacterial outer membrane. TamB, a component of this system spans the periplasmic space to engage with its partner protein TamA. Despite efforts to characterize the TAM, the structure and mechanism of action of TamB remained enigmatic. Here we present the crystal structure of TamB amino acids 963-1,138. This region represents half of the conserved DUF490 domain, the defining feature of TamB. TamB963-1138 consists of a concave, taco-shaped beta sheet with a hydrophobic interior. This beta taco structure is of dimensions capable of accommodating and shielding the hydrophobic side of an amphipathic beta strand, potentially allowing TamB to chaperone nascent membrane proteins from the aqueous environment. In addition, sequence analysis suggests that the structure of TamB963-1138 is shared by a large portion of TamB. This architecture could allow TamB to act as a conduit for membrane proteins.
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| - | The Structure of a Conserved Domain of TamB Reveals a Hydrophobic beta Taco Fold.,Josts I, Stubenrauch CJ, Vadlamani G, Mosbahi K, Walker D, Lithgow T, Grinter R Structure. 2017 Nov 3. pii: S0969-2126(17)30330-1. doi:, 10.1016/j.str.2017.10.002. PMID:29129383<ref>PMID:29129383</ref>
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| - | </div>
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| - | <div class="pdbe-citations 5vtg" style="background-color:#fffaf0;"></div>
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| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Ecoli]] | + | [[Category: Escherichia coli K-12]] |
| - | [[Category: Grinter, R]] | + | [[Category: Large Structures]] |
| - | [[Category: Josts, I]] | + | [[Category: Grinter R]] |
| - | [[Category: Beta-sheet]] | + | [[Category: Josts I]] |
| - | [[Category: Chaperone]]
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| - | [[Category: Periplasm]]
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| Structural highlights
Function
TAMB_ECOLI Part of the translocation and assembly module (TAM) autotransporter assembly complex, which functions in translocation of autotransporters across the outer membrane (PubMed:22466966). In reconstituted TAM this subunit (Ag43, AC P39180) is not necessary for substrate penetration in the outer membrane. Substrate binding to TamA moves its POTRA domains about 30 Angstroms into the periplasm, which would deform either the outer membrane or TamB and may provide force to reset TAM (PubMed:25341963).[1] [2]
References
- ↑ Selkrig J, Mosbahi K, Webb CT, Belousoff MJ, Perry AJ, Wells TJ, Morris F, Leyton DL, Totsika M, Phan MD, Celik N, Kelly M, Oates C, Hartland EL, Robins-Browne RM, Ramarathinam SH, Purcell AW, Schembri MA, Strugnell RA, Henderson IR, Walker D, Lithgow T. Discovery of an archetypal protein transport system in bacterial outer membranes. Nat Struct Mol Biol. 2012 Apr 1;19(5):506-10, S1. doi: 10.1038/nsmb.2261. PMID:22466966 doi:10.1038/nsmb.2261
- ↑ Shen HH, Leyton DL, Shiota T, Belousoff MJ, Noinaj N, Lu J, Holt SA, Tan K, Selkrig J, Webb CT, Buchanan SK, Martin LL, Lithgow T. Reconstitution of a nanomachine driving the assembly of proteins into bacterial outer membranes. Nat Commun. 2014 Oct 24;5:5078. doi: 10.1038/ncomms6078. PMID:25341963 doi:http://dx.doi.org/10.1038/ncomms6078
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