1tm6

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[[Image:1tm6.gif|left|200px]]
 
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{{Structure
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==NMR Structure of the Free Zinc Binding C-terminal Domain of SecA==
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|PDB= 1tm6 |SIZE=350|CAPTION= <scene name='initialview01'>1tm6</scene>
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<StructureSection load='1tm6' size='340' side='right'caption='[[1tm6]]' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>
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<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>
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|ACTIVITY=
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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|GENE=
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<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>
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|DOMAIN=
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<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>
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|RELATEDENTRY=
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1tm6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tm6 OCA], [http://www.ebi.ac.uk/pdbsum/1tm6 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1tm6 RCSB]</span>
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== Function ==
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}}
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[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>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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'''NMR Structure of the Free Zinc Binding C-terminal Domain of SecA'''
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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>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1tm6" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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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.
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*[[Preprotein translocase 3D structures|Preprotein translocase 3D structures]]
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*[[SecA|SecA]]
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==About this Structure==
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== References ==
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1TM6 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TM6 OCA].
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<references/>
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__TOC__
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==Reference==
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</StructureSection>
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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:[http://www.ncbi.nlm.nih.gov/pubmed/15488768 15488768]
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Alexandrescu, A T.]]
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[[Category: Alexandrescu AT]]
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[[Category: Matousek, W M.]]
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[[Category: Matousek WM]]
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[[Category: beta hairpin]]
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[[Category: seca]]
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[[Category: zinc finger]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:58:02 2008''
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Current revision

NMR Structure of the Free Zinc Binding C-terminal Domain of SecA

PDB ID 1tm6

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