View source for 2ltq


==High resolution structure of DsbB C41S by joint calculation with solid-state NMR and X-ray data==
<StructureSection load='2ltq' size='340' side='right'caption='[[2ltq]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2ltq]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LTQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LTQ FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solid-state NMR, 10 models</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=UQ8:UBIQUINONE-8'>UQ8</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=2ltq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ltq OCA], [https://pdbe.org/2ltq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ltq RCSB], [https://www.ebi.ac.uk/pdbsum/2ltq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ltq ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The integral membrane protein DsbB in Escherichia coli is responsible for oxidizing the periplasmic protein DsbA, which forms disulfide bonds in substrate proteins. We have developed a high-resolution structural model by combining experimental X-ray and solid-state NMR with molecular dynamics (MD) simulations. We embedded the high-resolution DsbB structure, derived from the joint calculation with X-ray reflections and solid-state NMR restraints, into the lipid bilayer and performed MD simulations to provide a mechanistic view of DsbB function in the membrane. Further, we revealed the membrane topology of DsbB by selective proton spin diffusion experiments, which directly probe the correlations of DsbB with water and lipid acyl chains. NMR data also support the model of a flexible periplasmic loop and an interhelical hydrogen bond between Glu26 and Tyr153.

Structure of the Disulfide Bond Generating Membrane Protein DsbB in the Lipid Bilayer.,Tang M, Nesbitt AE, Sperling LJ, Berthold DA, Schwieters CD, Gennis RB, Rienstra CM J Mol Biol. 2013 Feb 14. pii: S0022-2836(13)00095-8. doi:, 10.1016/j.jmb.2013.02.009. PMID:23416557<ref>PMID:23416557</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 2ltq" style="background-color:#fffaf0;"></div>

==See Also==
*[[Thiol:disulfide interchange protein 3D structures|Thiol:disulfide interchange protein 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Escherichia coli K-12]]
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Gennis RB]]
[[Category: Nesbitt AE]]
[[Category: Rienstra CM]]
[[Category: Schwieters CD]]
[[Category: Sperling LJ]]
[[Category: Tang M]]