1vrs
From Proteopedia
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| - | [[ | + | ==Crystal structure of the disulfide-linked complex between the N-terminal and C-terminal domain of the electron transfer catalyst DsbD== |
| + | <StructureSection load='1vrs' size='340' side='right' caption='[[1vrs]], [[Resolution|resolution]] 2.85Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[1vrs]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli_str._k-12_substr._w3110 Escherichia coli str. k-12 substr. w3110]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1se1 1se1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VRS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1VRS FirstGlance]. <br> | ||
| + | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">DSBD, DIPZ, CYCZ, CUTA2, B4136 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=316407 Escherichia coli str. K-12 substr. W3110])</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=1vrs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vrs OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1vrs RCSB], [http://www.ebi.ac.uk/pdbsum/1vrs PDBsum]</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] | ||
| + | == Evolutionary Conservation == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/vr/1vrs_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | DsbD from Escherichia coli catalyzes the transport of electrons from cytoplasmic thioredoxin to the periplasmic disulfide isomerase DsbC. DsbD contains two periplasmically oriented domains at the N- and C-terminus (nDsbD and cDsbD) that are connected by a central transmembrane (TM) domain. Each domain contains a pair of cysteines that are essential for catalysis. Here, we show that Cys109 and Cys461 form a transient interdomain disulfide bond between nDsbD and cDsbD in the reaction cycle of DsbD. We solved the crystal structure of this catalytic intermediate at 2.85 A resolution, which revealed large relative domain movements in DsbD as a consequence of a strong overlap between the surface areas of nDsbD that interact with DsbC and cDsbD. In addition, we have measured the kinetics of all functional and nonfunctional disulfide exchange reactions between redox-active, periplasmic proteins and protein domains from the oxidative DsbA/B and the reductive DsbC/D pathway. We show that both pathways are separated by large kinetic barriers for nonfunctional disulfide exchange between components from different pathways. | ||
| - | + | Structural basis and kinetics of inter- and intramolecular disulfide exchange in the redox catalyst DsbD.,Rozhkova A, Stirnimann CU, Frei P, Grauschopf U, Brunisholz R, Grutter MG, Capitani G, Glockshuber R EMBO J. 2004 Apr 21;23(8):1709-19. Epub 2004 Apr 1. PMID:15057279<ref>PMID:15057279</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| - | + | <references/> | |
| - | + | __TOC__ | |
| - | + | </StructureSection> | |
| - | + | ||
| - | == | + | |
| - | < | + | |
[[Category: Escherichia coli str. k-12 substr. w3110]] | [[Category: Escherichia coli str. k-12 substr. w3110]] | ||
[[Category: Protein-disulfide reductase]] | [[Category: Protein-disulfide reductase]] | ||
| - | [[Category: Brunisholz, R | + | [[Category: Brunisholz, R]] |
| - | [[Category: Capitani, G | + | [[Category: Capitani, G]] |
| - | [[Category: Frei, P | + | [[Category: Frei, P]] |
| - | [[Category: Glockshuber, R | + | [[Category: Glockshuber, R]] |
| - | [[Category: Grauschopf, U | + | [[Category: Grauschopf, U]] |
| - | [[Category: Gruetter, M G | + | [[Category: Gruetter, M G]] |
| - | [[Category: Rozhkova, A | + | [[Category: Rozhkova, A]] |
| - | [[Category: Stirnimann, C U | + | [[Category: Stirnimann, C U]] |
[[Category: Disulfide-linked]] | [[Category: Disulfide-linked]] | ||
[[Category: Dsbd]] | [[Category: Dsbd]] | ||
Revision as of 20:15, 25 December 2014
Crystal structure of the disulfide-linked complex between the N-terminal and C-terminal domain of the electron transfer catalyst DsbD
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