3pfu: Difference between revisions
From Proteopedia
Jump to navigationJump to search
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
==N-terminal domain of Thiol:disulfide interchange protein DsbD in its reduced form== | |||
<StructureSection load='3pfu' size='340' side='right' caption='[[3pfu]], [[Resolution|resolution]] 1.80Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3pfu]] is a 1 chain structure with sequence from [http://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=3PFU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3PFU FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DTT:2,3-DIHYDROXY-1,4-DITHIOBUTANE'>DTT</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1l6p|1l6p]], [[1jpe|1jpe]], [[1vrs|1vrs]]</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 Escherichia coli K-12])</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=3pfu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3pfu OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3pfu RCSB], [http://www.ebi.ac.uk/pdbsum/3pfu PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Bacterial growth and pathogenicity depend on the correct formation of disulfide bonds, a process controlled by the Dsb system in the periplasm of Gram-negative bacteria. Proteins with a thioredoxin fold play a central role in this process. A general feature of thiol-disulfide exchange reactions is the need to avoid a long lived product complex between protein partners. We use a multidisciplinary approach, involving NMR, x-ray crystallography, surface plasmon resonance, mutagenesis, and in vivo experiments, to investigate the interaction between the two soluble domains of the transmembrane reductant conductor DsbD. Our results show oxidation state-dependent affinities between these two domains. These observations have implications for the interactions of the ubiquitous thioredoxin-like proteins with their substrates, provide insight into the key role played by a unique redox partner with an immunoglobulin fold, and are of general importance for oxidative protein-folding pathways in all organisms. | |||
Oxidation state-dependent protein-protein interactions in disulfide cascades.,Mavridou DA, Saridakis E, Kritsiligkou P, Goddard AD, Stevens JM, Ferguson SJ, Redfield C J Biol Chem. 2011 Jul 15;286(28):24943-56. Epub 2011 May 3. PMID:21543317<ref>PMID:21543317</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Escherichia coli k-12]] | [[Category: Escherichia coli k-12]] | ||
[[Category: Protein-disulfide reductase]] | [[Category: Protein-disulfide reductase]] | ||
[[Category: Ferguson, S J | [[Category: Ferguson, S J]] | ||
[[Category: Mavridou, D A.I | [[Category: Mavridou, D A.I]] | ||
[[Category: Redfield, C | [[Category: Redfield, C]] | ||
[[Category: Saridakis, E | [[Category: Saridakis, E]] | ||
[[Category: Electron transport]] | [[Category: Electron transport]] | ||
[[Category: Immunoglobulin-like fold]] | [[Category: Immunoglobulin-like fold]] | ||
Revision as of 07:06, 19 December 2014
N-terminal domain of Thiol:disulfide interchange protein DsbD in its reduced form
| ||||||||||||
