2ltq

From Proteopedia

(Difference between revisions)

Revision as of 13:10, 22 February 2023

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 Escherichia coli K-12 and Mus musculus. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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 1: / Line 1: @@
 ==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]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''>
+<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/Ecoli Ecoli] 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>
+<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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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"><div style='overflow: auto; max-height: 3em;'>[[2leg|2leg]], [[2zuq|2zuq]]</div></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">b1185, dsbB, JW5182, roxB, ycgA ([https://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'>[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>
 == Function ==
-[[https://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>
+[https://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 27: / Line 25: @@
 __TOC__
 </StructureSection>
-[[Category: Ecoli]]
+[[Category: Escherichia coli K-12]]
 [[Category: Large Structures]]
 [[Category: Mus musculus]]
-[[Category: Gennis, R B]]
+[[Category: Gennis RB]]
-[[Category: Nesbitt, A E]]
+[[Category: Nesbitt AE]]
-[[Category: Rienstra, C M]]
+[[Category: Rienstra CM]]
-[[Category: Schwieters, C D]]
+[[Category: Schwieters CD]]
-[[Category: Sperling, L J]]
+[[Category: Sperling LJ]]
-[[Category: Tang, M]]
+[[Category: Tang M]]
-[[Category: Cell inner membrane]]
-[[Category: Cell membrane]]
-[[Category: Chaperone]]
-[[Category: Disulfide bond]]
-[[Category: Electron transport]]
-[[Category: Membrane]]
-[[Category: Membrane protein]]
-[[Category: Oxidoreductase]]
-[[Category: Redox-active center]]
-[[Category: Transmembrane]]
-[[Category: Transport]]

2ltq

From Proteopedia

Revision as of 13:10, 22 February 2023

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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