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| | <StructureSection load='4hts' size='340' side='right'caption='[[4hts]], [[Resolution|resolution]] 4.00Å' scene=''> | | <StructureSection load='4hts' size='340' side='right'caption='[[4hts]], [[Resolution|resolution]] 4.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4hts]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Aquae Aquae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HTS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4HTS FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4hts]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Aquifex_aeolicus_VF5 Aquifex aeolicus VF5]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HTS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4HTS FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4htt|4htt]]</td></tr> | + | </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=4hts FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hts OCA], [https://pdbe.org/4hts PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4hts RCSB], [https://www.ebi.ac.uk/pdbsum/4hts PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4hts ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">tatC, aq_1267 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=224324 AQUAE])</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=4hts FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hts OCA], [http://pdbe.org/4hts PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4hts RCSB], [http://www.ebi.ac.uk/pdbsum/4hts PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4hts ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/TATC_AQUAE TATC_AQUAE]] Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes (By similarity). | + | [https://www.uniprot.org/uniprot/TATC_AQUAE TATC_AQUAE] Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes (By similarity). |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Aquae]] | + | [[Category: Aquifex aeolicus VF5]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Chartron, J W]] | + | [[Category: Chartron JW]] |
| - | [[Category: Clemons, W M]] | + | [[Category: Clemons Jr WM]] |
| - | [[Category: Ramasamy, S]] | + | [[Category: Ramasamy S]] |
| - | [[Category: Protein transport]]
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| - | [[Category: Twin arginine translocase receptor]]
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| Structural highlights
Function
TATC_AQUAE Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes (By similarity).
Publication Abstract from PubMed
In bacteria, two signal-sequence-dependent secretion pathways translocate proteins across the cytoplasmic membrane. Although the mechanism of the ubiquitous general secretory pathway is becoming well understood, that of the twin-arginine translocation pathway, responsible for translocation of folded proteins across the bilayer, is more mysterious. TatC, the largest and most conserved of three integral membrane components, provides the initial binding site of the signal sequence prior to pore assembly. Here, we present two crystal structures of TatC from the thermophilic bacteria Aquifex aeolicus at 4.0 A and 6.8 A resolution. The membrane architecture of TatC includes a glove-shaped structure with a lipid-exposed pocket predicted by molecular dynamics to distort the membrane. Correlating the biochemical literature to these results suggests that the signal sequence binds in this pocket, leading to structural changes that facilitate higher order assemblies.
The Glove-like Structure of the Conserved Membrane Protein TatC Provides Insight into Signal Sequence Recognition in Twin-Arginine Translocation.,Ramasamy S, Abrol R, Suloway CJ, Clemons WM Jr Structure. 2013 Apr 9. pii: S0969-2126(13)00085-3. doi:, 10.1016/j.str.2013.03.004. PMID:23583035[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Ramasamy S, Abrol R, Suloway CJ, Clemons WM Jr. The Glove-like Structure of the Conserved Membrane Protein TatC Provides Insight into Signal Sequence Recognition in Twin-Arginine Translocation. Structure. 2013 Apr 9. pii: S0969-2126(13)00085-3. doi:, 10.1016/j.str.2013.03.004. PMID:23583035 doi:10.1016/j.str.2013.03.004
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