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2zup

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Revision as of 09:43, 12 October 2017

Updated crystal structure of DsbB-DsbA complex from E. coli

Structural highlights

2zup is a 2 chain structure with sequence from Ecoli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Related:	2hi7, 2zuq
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[DSBA_ECOLI] Required for disulfide bond formation in some periplasmic proteins such as PhoA or OmpA. Acts by transferring its disulfide bond to other proteins and is reduced in the process. DsbA is reoxidized by DsbB. Required for pilus biogenesis. PhoP-regulated transcription is redox-sensitive, being activated when the periplasm becomes more reducing (deletion of dsbA/dsbB, treatment with dithiothreitol). MgrB acts between DsbA/DsbB and PhoP/PhoQ in this pathway.^[1] ^[2] [DSBB_ECOLI] Required for disulfide bond formation in some periplasmic proteins such as PhoA or OmpA. Acts by oxidizing the DsbA protein.^[3] ^[4]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

In the Escherichia coli system catalysing oxidative protein folding, disulphide bonds are generated by the cooperation of DsbB and ubiquinone and transferred to substrate proteins through DsbA. The structures solved so far for different forms of DsbB lack the Cys104-Cys130 initial-state disulphide that is directly donated to DsbA. Here, we report the 3.4 A crystal structure of a DsbB-Fab complex, in which DsbB has this principal disulphide. Its comparison with the updated structure of the DsbB-DsbA complex as well as with the recently reported NMR structure of a DsbB variant having the rearranged Cys41-Cys130 disulphide illuminated conformational transitions of DsbB induced by the binding and release of DsbA. Mutational studies revealed that the membrane-parallel short alpha-helix of DsbB has a key function in physiological electron flow, presumably by controlling the positioning of the Cys130-containing loop. These findings demonstrate that DsbB has developed the elaborate conformational dynamism to oxidize DsbA for continuous protein disulphide bond formation in the cell.

Dynamic nature of disulphide bond formation catalysts revealed by crystal structures of DsbB.,Inaba K, Murakami S, Nakagawa A, Iida H, Kinjo M, Ito K, Suzuki M EMBO J. 2009 Mar 18;28(6):779-91. Epub 2009 Feb 12. PMID:19214188^[5]

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

References

↑ Akiyama Y, Kamitani S, Kusukawa N, Ito K. In vitro catalysis of oxidative folding of disulfide-bonded proteins by the Escherichia coli dsbA (ppfA) gene product. J Biol Chem. 1992 Nov 5;267(31):22440-5. PMID:1429594
↑ Lippa AM, Goulian M. Perturbation of the oxidizing environment of the periplasm stimulates the PhoQ/PhoP system in Escherichia coli. J Bacteriol. 2012 Mar;194(6):1457-63. doi: 10.1128/JB.06055-11. Epub 2012 Jan 20. PMID:22267510 doi:http://dx.doi.org/10.1128/JB.06055-11
↑ 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
↑ Inaba K, Murakami S, Nakagawa A, Iida H, Kinjo M, Ito K, Suzuki M. Dynamic nature of disulphide bond formation catalysts revealed by crystal structures of DsbB. EMBO J. 2009 Mar 18;28(6):779-91. Epub 2009 Feb 12. PMID:19214188 doi:10.1038/emboj.2009.21

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

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

@@ Line 1: / Line 1: @@
 ==Updated crystal structure of DsbB-DsbA complex from E. coli==
 <StructureSection load='2zup' size='340' side='right' caption='[[2zup]], [[Resolution|resolution]] 3.70&Aring;' scene=''>
@@ Line 5: / Line 6: @@
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=UQ1:UBIQUINONE-1'>UQ1</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2hi7|2hi7]], [[2zuq|2zuq]]</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=2zup FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zup OCA], [http://pdbe.org/2zup PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2zup RCSB], [http://www.ebi.ac.uk/pdbsum/2zup 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=2zup FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zup OCA], [http://pdbe.org/2zup PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2zup RCSB], [http://www.ebi.ac.uk/pdbsum/2zup PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2zup ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 28: / Line 29: @@
 </div>
 <div class="pdbe-citations 2zup" style="background-color:#fffaf0;"></div>
-==See Also==
-*[[Protein disulfide oxidoreductase|Protein disulfide oxidoreductase]]
 == References ==
 <references/>
@@ Line 49: / Line 47: @@
 [[Category: Membrane protein]]
 [[Category: Oxidoreductase]]
+[[Category: Periplasm]]
 [[Category: Redox-active center]]
 [[Category: Transmembrane]]
 [[Category: Transport]]

2zup

From Proteopedia

Revision as of 09:43, 12 October 2017

Updated crystal structure of DsbB-DsbA complex from E. coli

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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