4ip1: Difference between revisions
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==C-terminal domain of the thiol:disulfide interchange protein DsbD, Q488K mutant== | |||
<StructureSection load='4ip1' size='340' side='right'caption='[[4ip1]], [[Resolution|resolution]] 2.47Å' scene=''> | |||
== Structural highlights == | |||
<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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.47Å</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> | |||
</table> | |||
== Function == | |||
[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 == | |||
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<ref>PMID:24469455</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</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: Escherichia coli K-12]] | |||
[[Category: Large Structures]] | |||
[[Category: Mavridou DAI]] | |||
[[Category: Redfield C]] | |||
[[Category: Saridakis E]] | |||
