2ltq

From Proteopedia

(Difference between revisions)

Revision as of 02:38, 10 September 2015

High resolution structure of DsbB C41S by joint calculation with solid-state NMR and X-ray data

Structural highlights

2ltq is a 6 chain structure with sequence from Ecoli and Mus musculus. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	2leg, 2zuq
Gene:	b1185, dsbB, JW5182, roxB, ycgA (ECOLI)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum

Warning: this is a large structure, and loading might take a long time or not happen at all.

Function

[DSBB_ECOLI] Required for disulfide bond formation in some periplasmic proteins such as PhoA or OmpA. Acts by oxidizing the DsbA protein.^[1] ^[2]

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^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Bardwell JC, Lee JO, Jander G, Martin N, Belin D, Beckwith J. A pathway for disulfide bond formation in vivo. Proc Natl Acad Sci U S A. 1993 Feb 1;90(3):1038-42. PMID:8430071
↑ Missiakas D, Georgopoulos C, Raina S. Identification and characterization of the Escherichia coli gene dsbB, whose product is involved in the formation of disulfide bonds in vivo. Proc Natl Acad Sci U S A. 1993 Aug 1;90(15):7084-8. PMID:7688471
↑ Tang M, Nesbitt AE, Sperling LJ, Berthold DA, Schwieters CD, Gennis RB, Rienstra CM. Structure of the Disulfide Bond Generating Membrane Protein DsbB in the Lipid Bilayer. J Mol Biol. 2013 Feb 14. pii: S0022-2836(13)00095-8. doi:, 10.1016/j.jmb.2013.02.009. PMID:23416557 doi:10.1016/j.jmb.2013.02.009

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2ltq"

@@ Line 2: / Line 2: @@
 <StructureSection load='2ltq' size='340' side='right' caption='[[2ltq]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2ltq]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli_k-12 Escherichia coli k-12] and [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2LTQ FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2ltq]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecoli Ecoli] and [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2LTQ FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=UQ1:UBIQUINONE-1'>UQ1</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2leg|2leg]], [[2zuq|2zuq]]</td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">b1185, dsbB, JW5182, roxB, ycgA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 Escherichia coli K-12])</td></tr>
+<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">b1185, dsbB, JW5182, roxB, ycgA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</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=2ltq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ltq OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2ltq RCSB], [http://www.ebi.ac.uk/pdbsum/2ltq PDBsum]</span></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=2ltq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ltq OCA], [http://pdbe.org/2ltq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2ltq RCSB], [http://www.ebi.ac.uk/pdbsum/2ltq PDBsum]</span></td></tr>
 </table>
+{{Large structure}}
+== Function ==
+[[http://www.uniprot.org/uniprot/DSBB_ECOLI DSBB_ECOLI]] Required for disulfide bond formation in some periplasmic proteins such as PhoA or OmpA. Acts by oxidizing the DsbA protein.<ref>PMID:8430071</ref> <ref>PMID:7688471</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 16: / Line 19: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 2ltq" style="background-color:#fffaf0;"></div>
 ==See Also==
@@ Line 23: / Line 27: @@
 __TOC__
 </StructureSection>
-[[Category: Escherichia coli k-12]]
+[[Category: Ecoli]]
 [[Category: Mus musculus]]
 [[Category: Gennis, R B]]

2ltq

From Proteopedia

Revision as of 02:38, 10 September 2015

High resolution structure of DsbB C41S by joint calculation with solid-state NMR and X-ray data

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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