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4ip6

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Revision as of 08:54, 5 August 2016

C-terminal domain of the thiol:disulfide interchange protein DsbD, Q488A mutant

Structural highlights

4ip6 is a 1 chain structure with sequence from Ecoli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	4ip1
Gene:	dsbD, cutA2, cycZ, dipZ, b4136, JW5734 (ECOLI)
Activity:	Protein-disulfide reductase, with EC number 1.8.1.8
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/4ip6"

@@ Line 1: / Line 1: @@
 ==C-terminal domain of the thiol:disulfide interchange protein DsbD, Q488A mutant==
 <StructureSection load='4ip6' size='340' side='right' caption='[[4ip6]], [[Resolution|resolution]] 2.23&Aring;' scene=''>
@@ Line 6: / Line 7: @@
 <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='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=4ip6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ip6 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ip6 RCSB], [http://www.ebi.ac.uk/pdbsum/4ip6 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=4ip6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ip6 OCA], [http://pdbe.org/4ip6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ip6 RCSB], [http://www.ebi.ac.uk/pdbsum/4ip6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4ip6 ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 18: / Line 19: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 4ip6" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Thiol:disulfide interchange protein|Thiol:disulfide interchange protein]]
 == References ==
 <references/>

4ip6

From Proteopedia

Revision as of 08:54, 5 August 2016

C-terminal domain of the thiol:disulfide interchange protein DsbD, Q488A mutant

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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