4b4a: Difference between revisions
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<StructureSection load='4b4a' size='340' side='right'caption='[[4b4a]], [[Resolution|resolution]] 3.50Å' scene=''> | <StructureSection load='4b4a' size='340' side='right'caption='[[4b4a]], [[Resolution|resolution]] 3.50Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4b4a]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[4b4a]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"aquifex_aeolicus"_huber_and_stetter_2001 "aquifex aeolicus" huber and stetter 2001]. 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 [https://proteopedia.org/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> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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='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'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4b4a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4b4a OCA], [https://pdbe.org/4b4a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4b4a RCSB], [https://www.ebi.ac.uk/pdbsum/4b4a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4b4a ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[ | [[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 == |
Latest revision as of 09:59, 31 August 2022
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
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 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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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)
OCA- Aquifex aeolicus huber and stetter 2001
- Large Structures
- Berks, B C
- Graham, J E
- Hogbom, M
- Jaaskelainen, M
- Jaeger, F
- Johnson, S
- Krehenbrink, M
- Lea, S M
- Liu, S M
- Lukey, M J
- Marcoux, J
- McDowell, M A
- Palmer, T
- Robinson, C V
- Rollauer, S E
- Roversi, P
- Sansom, M S
- Stansfeld, P J
- Tarry, M J
- Protein translocation
- Tat secretion system
- Transport protein