2lzs
From Proteopedia
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| - | + | ==TatA oligomer== | |
| - | === | + | <StructureSection load='2lzs' size='340' side='right' caption='[[2lzs]], [[NMR_Ensembles_of_Models | 1 NMR models]]' scene=''> |
| - | + | == Structural highlights == | |
| + | <table><tr><td colspan='2'>[[2lzs]] is a 9 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli_k-12 Escherichia coli k-12]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LZS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2LZS FirstGlance]. <br> | ||
| + | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=FME:N-FORMYLMETHIONINE'>FME</scene></td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">tatA, mttA1, yigT, b3836, JW3813 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 Escherichia coli K-12])</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=2lzs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lzs OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2lzs RCSB], [http://www.ebi.ac.uk/pdbsum/2lzs PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The twin-arginine translocase (Tat) carries out the remarkable process of translocating fully folded proteins across the cytoplasmic membrane of prokaryotes and the thylakoid membrane of plant chloroplasts. Tat is required for bacterial pathogenesis and for photosynthesis in plants. TatA, the protein-translocating element of the Tat system, is a small transmembrane protein that assembles into ring-like oligomers of variable size. We have determined a structural model of the Escherichia coli TatA complex in detergent solution by NMR. TatA assembly is mediated entirely by the transmembrane helix. The amphipathic helix extends outwards from the ring of transmembrane helices, permitting assembly of complexes with variable subunit numbers. Transmembrane residue Gln8 points inward, resulting in a short hydrophobic pore in the center of the complex. Simulations of the TatA complex in lipid bilayers indicate that the short transmembrane domain distorts the membrane. This finding suggests that TatA facilitates protein transport by sensitizing the membrane to transient rupture. | ||
| - | + | Structural model for the protein-translocating element of the twin-arginine transport system.,Rodriguez F, Rouse SL, Tait CE, Harmer J, De Riso A, Timmel CR, Sansom MS, Berks BC, Schnell JR Proc Natl Acad Sci U S A. 2013 Mar 7. PMID:23471988<ref>PMID:23471988</ref> | |
| - | + | ||
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| - | == | + | <references/> |
| - | <references | + | __TOC__ |
| + | </StructureSection> | ||
[[Category: Escherichia coli k-12]] | [[Category: Escherichia coli k-12]] | ||
| - | [[Category: Berks, B C | + | [[Category: Berks, B C]] |
| - | [[Category: Rodriguez, F M | + | [[Category: Rodriguez, F M]] |
| - | [[Category: Schnell, J R | + | [[Category: Schnell, J R]] |
[[Category: Dpc]] | [[Category: Dpc]] | ||
[[Category: Membrane protein]] | [[Category: Membrane protein]] | ||
[[Category: Protein transport]] | [[Category: Protein transport]] | ||
[[Category: Tata]] | [[Category: Tata]] | ||
Revision as of 11:45, 18 December 2014
TatA oligomer
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