1tm6: Difference between revisions
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==NMR Structure of the Free Zinc Binding C-terminal Domain of SecA== | |||
<StructureSection load='1tm6' size='340' side='right'caption='[[1tm6]]' scene=''> | |||
| | == Structural highlights == | ||
| | <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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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'>[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> | |||
== 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 an integral component of the prokaryotic Sec preprotein secretory translocase system. We report here the solution NMR structure of a fragment corresponding to the C-terminal domain of Escherichia coli SecA. In the presence of Zn2+, the fragment adopts a shortened version of the classic betabetaalpha zinc finger fold. The isolated C-terminal domain shows substantial differences from the X-ray structure of a homologous SecA domain bound to the chaperone-like cofactor SecB. The differences between the structures of the free and bound forms suggest that binding to SecB causes a perturbation of the C-terminal domain's intrinsically favored betabetaalpha fold. | |||
NMR structure of the C-terminal domain of SecA in the free state.,Matousek WM, Alexandrescu AT Biochim Biophys Acta. 2004 Nov 1;1702(2):163-71. PMID:15488768<ref>PMID:15488768</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1tm6" style="background-color:#fffaf0;"></div> | |||
== | ==See Also== | ||
*[[Preprotein translocase 3D structures|Preprotein translocase 3D structures]] | |||
*[[SecA|SecA]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
== | </StructureSection> | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Alexandrescu | [[Category: Alexandrescu AT]] | ||
[[Category: Matousek | [[Category: Matousek WM]] | ||
Latest revision as of 09:26, 6 December 2023
NMR Structure of the Free Zinc Binding C-terminal Domain of SecA
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