1tm6
From Proteopedia
(Difference between revisions)
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<StructureSection load='1tm6' size='340' side='right'caption='[[1tm6]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | <StructureSection load='1tm6' size='340' side='right'caption='[[1tm6]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[1tm6]] is a 1 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[1tm6]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TM6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TM6 FirstGlance]. <br> |
- | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</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=1tm6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tm6 OCA], [https://pdbe.org/1tm6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1tm6 RCSB], [https://www.ebi.ac.uk/pdbsum/1tm6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1tm6 ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
- | [[ | + | [[https://www.uniprot.org/uniprot/SECA_ECOLI SECA_ECOLI]] Required for protein export, interacts with the SecYEG preprotein conducting channel. SecA has a central role in coupling the hydrolysis of ATP to the transfer of proteins into and across the cell membrane, serving both as a receptor for the preprotein-SecB complex and as an ATP-driven molecular motor driving the stepwise translocation of polypeptide chains across the membrane.<ref>PMID:15140892</ref> |
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == |
Revision as of 09:29, 29 September 2021
NMR Structure of the Free Zinc Binding C-terminal Domain of SecA
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