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[[ | ==Structure of the TatC core of the twin arginine protein translocation system== | ||
<StructureSection load='4b4a' size='340' side='right' caption='[[4b4a]], [[Resolution|resolution]] 3.50Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4b4a]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Aquifex_aeolicus Aquifex aeolicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4B4A OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4B4A FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=LMN:LAURYL+MALTOSE+NEOPENTYL+GLYCOL'>LMN</scene></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> | |||
<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=4b4a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4b4a OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4b4a RCSB], [http://www.ebi.ac.uk/pdbsum/4b4a PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The twin-arginine translocation (Tat) pathway is one of two general protein transport systems found in the prokaryotic cytoplasmic membrane and is conserved in the thylakoid membrane of plant chloroplasts. The defining, and highly unusual, property of the Tat pathway is that it transports folded proteins, a task that must be achieved without allowing appreciable ion leakage across the membrane. The integral membrane TatC protein is the central component of the Tat pathway. TatC captures substrate proteins by binding their signal peptides. TatC then recruits TatA family proteins to form the active translocation complex. Here we report the crystal structure of TatC from the hyperthermophilic bacterium Aquifex aeolicus. This structure provides a molecular description of the core of the Tat translocation system and a framework for understanding the unique Tat transport mechanism. | |||
Structure of the TatC core of the twin-arginine protein transport system.,Rollauer SE, Tarry MJ, Graham JE, Jaaskelainen M, Jager F, Johnson S, Krehenbrink M, Liu SM, Lukey MJ, Marcoux J, McDowell MA, Rodriguez F, Roversi P, Stansfeld PJ, Robinson CV, Sansom MS, Palmer T, Hogbom M, Berks BC, Lea SM Nature. 2012 Dec 2. doi: 10.1038/nature11683. PMID:23201679<ref>PMID:23201679</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
<references/> | |||
== | __TOC__ | ||
</StructureSection> | |||
[[Category: Aquifex aeolicus]] | [[Category: Aquifex aeolicus]] | ||
[[Category: Berks, B C | [[Category: Berks, B C]] | ||
[[Category: Graham, J E | [[Category: Graham, J E]] | ||
[[Category: Hogbom, M | [[Category: Hogbom, M]] | ||
[[Category: Jaaskelainen, M | [[Category: Jaaskelainen, M]] | ||
[[Category: Jaeger, F | [[Category: Jaeger, F]] | ||
[[Category: Johnson, S | [[Category: Johnson, S]] | ||
[[Category: Krehenbrink, M | [[Category: Krehenbrink, M]] | ||
[[Category: Lea, S M | [[Category: Lea, S M]] | ||
[[Category: Liu, S M | [[Category: Liu, S M]] | ||
[[Category: Lukey, M J | [[Category: Lukey, M J]] | ||
[[Category: Marcoux, J | [[Category: Marcoux, J]] | ||
[[Category: Mcdowell, M A | [[Category: Mcdowell, M A]] | ||
[[Category: Palmer, T | [[Category: Palmer, T]] | ||
[[Category: Robinson, C V | [[Category: Robinson, C V]] | ||
[[Category: Rollauer, S E | [[Category: Rollauer, S E]] | ||
[[Category: Roversi, P | [[Category: Roversi, P]] | ||
[[Category: Sansom, M S | [[Category: Sansom, M S]] | ||
[[Category: Stansfeld, P J | [[Category: Stansfeld, P J]] | ||
[[Category: Tarry, M J | [[Category: Tarry, M J]] | ||
[[Category: Protein translocation]] | [[Category: Protein translocation]] | ||
[[Category: Tat secretion system]] | [[Category: Tat secretion system]] | ||
[[Category: Transport protein]] | [[Category: Transport protein]] | ||
Revision as of 19:28, 9 December 2014
Structure of the TatC core of the twin arginine protein translocation systemStructure of the TatC core of the twin arginine protein translocation system
Structural highlights
Publication Abstract from PubMedThe twin-arginine translocation (Tat) pathway is one of two general protein transport systems found in the prokaryotic cytoplasmic membrane and is conserved in the thylakoid membrane of plant chloroplasts. The defining, and highly unusual, property of the Tat pathway is that it transports folded proteins, a task that must be achieved without allowing appreciable ion leakage across the membrane. The integral membrane TatC protein is the central component of the Tat pathway. TatC captures substrate proteins by binding their signal peptides. TatC then recruits TatA family proteins to form the active translocation complex. Here we report the crystal structure of TatC from the hyperthermophilic bacterium Aquifex aeolicus. This structure provides a molecular description of the core of the Tat translocation system and a framework for understanding the unique Tat transport mechanism. Structure of the TatC core of the twin-arginine protein transport system.,Rollauer SE, Tarry MJ, Graham JE, Jaaskelainen M, Jager F, Johnson S, Krehenbrink M, Liu SM, Lukey MJ, Marcoux J, McDowell MA, Rodriguez F, Roversi P, Stansfeld PJ, Robinson CV, Sansom MS, Palmer T, Hogbom M, Berks BC, Lea SM Nature. 2012 Dec 2. doi: 10.1038/nature11683. PMID:23201679[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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