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4ihu

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Revision as of 20:46, 16 November 2022

Reduced form of disulfide bond oxdioreductase (DsbG) from Mycobacterium tuberculosis

Structural highlights

4ihu is a 2 chain structure with sequence from Mycobacterium tuberculosis H37Rv. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

O33272_MYCTU

Publication Abstract from PubMed

BACKGROUND: Bacterial Disulfide bond forming (Dsb) proteins facilitate proper folding and disulfide bond formation of periplasmic and secreted proteins. Previously, we have shown that Mycobacterium tuberculosis Mt-DsbE and Mt-DsbF aid in vitro oxidative folding of proteins. The M. tuberculosis proteome contains another predicted membrane-tethered Dsb protein, Mt-DsbA, which is encoded by an essential gene. RESULTS: Herein, we present structural and biochemical analyses of Mt-DsbA. The X-ray crystal structure of Mt-DsbA reveals a two-domain structure, comprising a canonical thioredoxin domain with the conserved CXXC active site cysteines in their reduced form, and an inserted alpha-helical domain containing a structural disulfide bond. The overall fold of Mt-DsbA resembles that of other DsbA-like proteins and not Mt-DsbE or Mt-DsbF. Biochemical characterization demonstrates that, unlike Mt-DsbE and Mt-DsbF, Mt-DsbA is unable to oxidatively fold reduced, denatured hirudin. Moreover, on the substrates tested in this study, Mt-DsbA has disulfide bond isomerase activity contrary to Mt-DsbE and Mt-DsbF. CONCLUSION: These results suggest that Mt-DsbA acts upon a distinct subset of substrates as compared to Mt-DsbE and Mt-DsbF. One could speculate that Mt-DsbE and Mt-DsbF are functionally redundant whereas Mt-DsbA is not, offering an explanation for the essentiality of Mt-DsbA in M. tuberculosis.

Structural and biochemical characterization of the essential DsbA-like disulfide bond forming protein from Mycobacterium tuberculosis.,Chim N, Harmston CA, Guzman DJ, Goulding CW BMC Struct Biol. 2013 Oct 18;13(1):23. PMID:24134223^[1]

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

References

↑ Chim N, Harmston CA, Guzman DJ, Goulding CW. Structural and biochemical characterization of the essential DsbA-like disulfide bond forming protein from Mycobacterium tuberculosis. BMC Struct Biol. 2013 Oct 18;13(1):23. PMID:24134223 doi:http://dx.doi.org/10.1186/1472-6807-13-23

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/4ihu"

Categories: Large Structures | Mycobacterium tuberculosis H37Rv | Goulding CW | Harmston CA

@@ Line 1: / Line 1: @@
 ==Reduced form of disulfide bond oxdioreductase (DsbG) from Mycobacterium tuberculosis==
-<StructureSection load='4ihu' size='340' side='right' caption='[[4ihu]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
+<StructureSection load='4ihu' size='340' side='right'caption='[[4ihu]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4ihu]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Myctu Myctu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4IHU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4IHU FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4ihu]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis_H37Rv Mycobacterium tuberculosis H37Rv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4IHU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4IHU FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
-<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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=4ihu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ihu OCA], [https://pdbe.org/4ihu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ihu RCSB], [https://www.ebi.ac.uk/pdbsum/4ihu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ihu ProSAT]</span></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Rv2969c ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83332 MYCTU])</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=4ihu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ihu OCA], [http://pdbe.org/4ihu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ihu RCSB], [http://www.ebi.ac.uk/pdbsum/4ihu PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4ihu ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/O33272_MYCTU O33272_MYCTU]
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 18: / Line 18: @@
 </div>
 <div class="pdbe-citations 4ihu" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Thiol:disulfide interchange protein 3D structures|Thiol:disulfide interchange protein 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Myctu]]
+[[Category: Large Structures]]
-[[Category: Goulding, C W]]
+[[Category: Mycobacterium tuberculosis H37Rv]]
-[[Category: Harmston, C A]]
+[[Category: Goulding CW]]
-[[Category: Disulfide bond isomerase]]
+[[Category: Harmston CA]]
-[[Category: Oxidoreductase]]
-[[Category: Redox]]
-[[Category: Thioredoxin]]

4ihu

From Proteopedia

Revision as of 20:46, 16 November 2022

Reduced form of disulfide bond oxdioreductase (DsbG) from Mycobacterium tuberculosis

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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