5k9t
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==SecA-N68, a C-terminal truncation of the SecA ATPase from E. coli== | |
| + | <StructureSection load='5k9t' size='340' side='right'caption='[[5k9t]], [[Resolution|resolution]] 2.60Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5k9t]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_55989 Escherichia coli 55989]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5K9T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5K9T FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></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=5k9t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5k9t OCA], [https://pdbe.org/5k9t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5k9t RCSB], [https://www.ebi.ac.uk/pdbsum/5k9t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5k9t ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == 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;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | SecA is the ATPase of preprotein translocase. SecA is a dimer in solution and changes in its oligomeric state may function in preprotein translocation. The SecA-N68 construct, in which the C-terminal helical domains of SecA are deleted, was used to investigate the mechanism of SecA oligomerization. SecA-N68 is in equilibrium between monomers, dimers, and tetramers. Subunit interactions in the SecA-N68 tetramer are mediated entirely by unstructured regions at its N- and C-termini: when the termini are deleted to yield SecA-N68NC, the construct is completely monomeric. This monomeric construct yielded crystals diffracting to 2.6 A that were used to solve the structure of SecA-N68, including the "preprotein crosslinking domain" (PPXD) that was missing from previous E. coli SecA structures. The SecA-N68 structure was combined with small angle X-ray scattering (SAXS) data to construct a model of the SecA-N68 tetramer that is consistent with the essential roles of the extreme N- and C-termini in oligomerization. This mode of oligomerization, which depends on binding of the extreme N-terminus to the DEAD motor domains, NBD1 and NBD2, was used to model a novel parallel and flexible SecA solution dimer that agrees well with SAXS data. | ||
| - | + | An alternate mode of oligomerization for E. coli SecA.,Yazdi AK, Vezina GC, Shilton BH Sci Rep. 2017 Sep 18;7(1):11747. doi: 10.1038/s41598-017-11648-5. PMID:28924213<ref>PMID:28924213</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 5k9t" style="background-color:#fffaf0;"></div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[SecA|SecA]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Escherichia coli 55989]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Shilton BH]] | ||
| + | [[Category: Vezina GC]] | ||
Current revision
SecA-N68, a C-terminal truncation of the SecA ATPase from E. coli
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