4ip6

From Proteopedia

(Difference between revisions)

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?)

Views

Personal tools

Navigation

Search

Toolbox