5k9t: Difference between revisions
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==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. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5K9T FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5k9t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5k9t OCA], [http://pdbe.org/5k9t PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5k9t RCSB], [http://www.ebi.ac.uk/pdbsum/5k9t PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5k9t ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[[http://www.uniprot.org/uniprot/SECA_ECO55 SECA_ECO55]] Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. 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. | |||
<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: Shilton, B H]] | |||
[[Category: Vezina, G C]] | |||
[[Category: Atpase]] | |||
[[Category: C-terminal truncation]] | |||
[[Category: N-terminus]] | |||
[[Category: Peptide binding]] | |||
[[Category: Preprotein translocase]] | |||
[[Category: Protein transport]] | |||
[[Category: Seca-n68]] | |||
