This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1tm6

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (09:26, 6 December 2023) (edit) (undo)
 
(12 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1tm6.gif|left|200px]]
 
-
{{Structure
+
==NMR Structure of the Free Zinc Binding C-terminal Domain of SecA==
-
|PDB= 1tm6 |SIZE=350|CAPTION= <scene name='initialview01'>1tm6</scene>
+
<StructureSection load='1tm6' size='340' side='right'caption='[[1tm6]]' scene=''>
-
|SITE=
+
== Structural highlights ==
-
|LIGAND= <scene name='pdbligand=ZN:ZINC ION'>ZN</scene>
+
<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>
-
|ACTIVITY=
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
-
|GENE=
+
<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 Free Zinc Binding C-terminal Domain of SecA'''
+
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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 +
</div>
 +
<div class="pdbe-citations 1tm6" style="background-color:#fffaf0;"></div>
-
==Overview==
+
==See Also==
-
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.
+
*[[Preprotein translocase 3D structures|Preprotein translocase 3D structures]]
-
 
+
*[[SecA|SecA]]
-
==About this Structure==
+
== References ==
-
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].
+
<references/>
-
 
+
__TOC__
-
==Reference==
+
</StructureSection>
-
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]
+
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
-
[[Category: Single protein]]
+
[[Category: Large Structures]]
-
[[Category: Alexandrescu, A T.]]
+
[[Category: Alexandrescu AT]]
-
[[Category: Matousek, W M.]]
+
[[Category: Matousek WM]]
-
[[Category: ZN]]
+
-
[[Category: beta hairpin]]
+
-
[[Category: seca]]
+
-
[[Category: zinc finger]]
+
-
 
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:20:14 2008''
+

Current revision

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

PDB ID 1tm6

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1tm6"
Personal tools