1un2

From Proteopedia

(Difference between revisions)

Current revision

Crystal structure of circularly permuted CPDSBA_Q100T99: Preserved Global Fold and Local Structural Adjustments

Structural highlights

1un2 is a 1 chain structure with sequence from Escherichia coli. This structure supersedes the now removed PDB entry 1dyv. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.4Å
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]

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

The thiol-disulfide oxidoreductase DsbA is required for efficient formation of disulfide bonds in the Escherichia coli periplasm. The enzyme is the strongest oxidant of the family of thioredoxin-like proteins and three-dimensional structures of both oxidized and reduced forms are known. DsbA consists of a catalytic thioredoxin-like domain and a helical domain that is inserted into the thioredoxin motif. Here, the X-ray structure of a circularly permuted variant, cpDsbA(Q100T99), is reported in which the natural termini are joined by the pentapeptide linker GGGTG, leading to a continuous thioredoxin domain, and new termini that have been introduced in the helical domain by breaking the peptide bond Thr99-Gln100. cpDsbA(Q100T99) is catalytically active in vivo and in vitro. The crystal structure of oxidized cpDsbA(Q100T99), determined by molecular replacement at 2.4 A resolution, was found to be very similar to that of wild-type DsbA. The lower thermodynamic stability of cpDsbA(Q100T99) relative to DsbA is associated with small structural changes within the molecule, especially near the new termini and the circularizing linker. The active-site helices and adjacent loops display increased flexibility compared with oxidized DsbA.

Structure of circularly permuted DsbA(Q100T99): preserved global fold and local structural adjustments.,Manjasetty BA, Hennecke J, Glockshuber R, Heinemann U Acta Crystallogr D Biol Crystallogr. 2004 Feb;60(Pt 2):304-9. Epub 2004, Jan 23. PMID:14747707^[3]

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
↑ Manjasetty BA, Hennecke J, Glockshuber R, Heinemann U. Structure of circularly permuted DsbA(Q100T99): preserved global fold and local structural adjustments. Acta Crystallogr D Biol Crystallogr. 2004 Feb;60(Pt 2):304-9. Epub 2004, Jan 23. PMID:14747707 doi:10.1107/S0907444903028695

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/1un2"

@@ Line 1: / Line 1: @@
-==CRYSTAL STRUCTURE OF CIRCULARLY PERMUTED CPDSBA_Q100T99 PRESERVED GLOBAL FOLD AND LOCAL STRUCTURAL ADJUSTMENTS==
-<StructureSection load='1un2' size='340' side='right' caption='[[1un2]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
+==Crystal structure of circularly permuted CPDSBA_Q100T99: Preserved Global Fold and Local Structural Adjustments==
+<StructureSection load='1un2' size='340' side='right'caption='[[1un2]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1un2]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1dyv 1dyv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UN2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1UN2 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1un2]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1dyv 1dyv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UN2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1UN2 FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1a23|1a23]], [[1a24|1a24]], [[1a2j|1a2j]], [[1a2l|1a2l]], [[1a2m|1a2m]], [[1ac1|1ac1]], [[1acv|1acv]], [[1bq7|1bq7]], [[1dsb|1dsb]], [[1fvj|1fvj]], [[1fvk|1fvk]]</td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;</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=1un2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1un2 OCA], [http://pdbe.org/1un2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1un2 RCSB], [http://www.ebi.ac.uk/pdbsum/1un2 PDBsum]</span></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=1un2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1un2 OCA], [https://pdbe.org/1un2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1un2 RCSB], [https://www.ebi.ac.uk/pdbsum/1un2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1un2 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/DSBA_ECOLI 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.<ref>PMID:1429594</ref> <ref>PMID:22267510</ref>
+[https://www.uniprot.org/uniprot/DSBA_ECOLI 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.<ref>PMID:1429594</ref> <ref>PMID:22267510</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/un/1un2_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/un/1un2_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
-</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1un2 ConSurf].
 <div style="clear:both"></div>
 <div style="background-color:#fffaf0;">
@@ Line 31: / Line 32: @@
 __TOC__
 </StructureSection>
-[[Category: Bacillus coli migula 1895]]
+[[Category: Escherichia coli]]
-[[Category: Glockshuber, R]]
+[[Category: Large Structures]]
-[[Category: Heinemann, U]]
+[[Category: Glockshuber R]]
-[[Category: Hennecke, J]]
+[[Category: Heinemann U]]
-[[Category: Manjasetty, B A]]
+[[Category: Hennecke J]]
-[[Category: Circular permutation]]
+[[Category: Manjasetty BA]]
-[[Category: Disulfide bond formation]]
-[[Category: Disulfide oxidoreductase]]
-[[Category: Oxidoreductase]]
-[[Category: Protein disulfide isomerase]]
-[[Category: Protein folding]]
-[[Category: Redox protein]]
-[[Category: Thioredoxin]]

1un2

From Proteopedia

Current revision

Crystal structure of circularly permuted CPDSBA_Q100T99: Preserved Global Fold and Local Structural Adjustments

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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