4ip1

From Proteopedia

(Difference between revisions)

Current revision

C-terminal domain of the thiol:disulfide interchange protein DsbD, Q488K mutant

Structural highlights

4ip1 is a 1 chain structure with sequence from Escherichia coli K-12. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.47Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

DSBD_ECOLI Required to facilitate the formation of correct disulfide bonds in some periplasmic proteins and for the assembly of the periplasmic c-type cytochromes. Acts by transferring electrons from cytoplasmic thioredoxin to the periplasm, thereby maintaining the active site of DsbC, DsbE and DsbG in a reduced state. This transfer involves a cascade of disulfide bond formation and reduction steps.[HAMAP-Rule:MF_00399]

Publication Abstract from PubMed

Proteins belonging to the thioredoxin superfamily are abundant in all organisms. They share the same structural features, arranged in a seemingly simple fold, but they perform a multitude of functions in oxidative protein folding and electron transfer pathways. We use the C-terminal domain of the unique transmembrane reductant conductor DsbD (cDsbD) as a model for an in-depth analysis of the factors controlling the reactivity of the Trx fold. We employ NMR spectroscopy, X-ray crystallography, mutagenesis, in vivo functional experiments applied to DsbD and a comparative sequence analysis of Trx-fold proteins to determine the effect of residues in the vicinity of the active site on the ionization of the key nucleophilic cysteine of the -CXXC- motif. We show that the function and reactivity of Trx-fold proteins depend critically on the electrostatic features imposed by an extended active-site motif.

An Extended Active-site Motif Controls the Reactivity of the Thioredoxin Fold.,Mavridou DA, Saridakis E, Kritsiligkou P, Mozley EC, Ferguson SJ, Redfield C J Biol Chem. 2014 Jan 27. PMID:24469455^[1]

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

References

↑ Mavridou DA, Saridakis E, Kritsiligkou P, Mozley EC, Ferguson SJ, Redfield C. An Extended Active-site Motif Controls the Reactivity of the Thioredoxin Fold. J Biol Chem. 2014 Jan 27. PMID:24469455 doi:http://dx.doi.org/10.1074/jbc.M113.513457

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/4ip1"

Categories: Escherichia coli K-12 | Large Structures | Mavridou DAI | Redfield C | Saridakis E

@@ Line 1: / Line 1: @@
 ==C-terminal domain of the thiol:disulfide interchange protein DsbD, Q488K mutant==
-<StructureSection load='4ip1' size='340' side='right' caption='[[4ip1]], [[Resolution|resolution]] 2.47&Aring;' scene=''>
+<StructureSection load='4ip1' size='340' side='right'caption='[[4ip1]], [[Resolution|resolution]] 2.47&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4ip1]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4IP1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4IP1 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4ip1]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4IP1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4IP1 FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4ip6|4ip6]]</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]] 2.47&#8491;</td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">dsbD, cutA2, cycZ, dipZ, b4136, JW5734 ([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'>[https://proteopedia.org/fgij/fg.htm?mol=4ip1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ip1 OCA], [https://pdbe.org/4ip1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ip1 RCSB], [https://www.ebi.ac.uk/pdbsum/4ip1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ip1 ProSAT]</span></td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Protein-disulfide_reductase Protein-disulfide reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.1.8 1.8.1.8] </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=4ip1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ip1 OCA], [http://pdbe.org/4ip1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ip1 RCSB], [http://www.ebi.ac.uk/pdbsum/4ip1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4ip1 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/DSBD_ECOLI DSBD_ECOLI]] Required to facilitate the formation of correct disulfide bonds in some periplasmic proteins and for the assembly of the periplasmic c-type cytochromes. Acts by transferring electrons from cytoplasmic thioredoxin to the periplasm, thereby maintaining the active site of DsbC, DsbE and DsbG in a reduced state. This transfer involves a cascade of disulfide bond formation and reduction steps.[HAMAP-Rule:MF_00399]
+[https://www.uniprot.org/uniprot/DSBD_ECOLI DSBD_ECOLI] Required to facilitate the formation of correct disulfide bonds in some periplasmic proteins and for the assembly of the periplasmic c-type cytochromes. Acts by transferring electrons from cytoplasmic thioredoxin to the periplasm, thereby maintaining the active site of DsbC, DsbE and DsbG in a reduced state. This transfer involves a cascade of disulfide bond formation and reduction steps.[HAMAP-Rule:MF_00399]
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 20: / Line 18: @@
 </div>
 <div class="pdbe-citations 4ip1" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Thiol:disulfide interchange protein 3D structures|Thiol:disulfide interchange protein 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Ecoli]]
+[[Category: Escherichia coli K-12]]
-[[Category: Protein-disulfide reductase]]
+[[Category: Large Structures]]
-[[Category: Mavridou, D A.I]]
+[[Category: Mavridou DAI]]
-[[Category: Redfield, C]]
+[[Category: Redfield C]]
-[[Category: Saridakis, E]]
+[[Category: Saridakis E]]
-[[Category: Bacterial periplasm]]
-[[Category: Oxidoreductase]]
-[[Category: Thiol:disulfide oxidoreductase]]
-[[Category: Thioredoxin]]

4ip1

From Proteopedia

Current revision

C-terminal domain of the thiol:disulfide interchange protein DsbD, Q488K mutant

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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