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==Crystal Structure of Neisseria meningitidis DsbD c-terminal domain in the oxidised form== | |||
<StructureSection load='6dnu' size='340' side='right' caption='[[6dnu]], [[Resolution|resolution]] 2.28Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6dnu]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6DNU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6DNU FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=P6G:HEXAETHYLENE+GLYCOL'>P6G</scene></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=6dnu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6dnu OCA], [http://pdbe.org/6dnu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6dnu RCSB], [http://www.ebi.ac.uk/pdbsum/6dnu PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6dnu ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[[http://www.uniprot.org/uniprot/C6S7X6_NEIML C6S7X6_NEIML]] 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. 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 == | |||
The membrane protein DsbD is a reductase that acts as an electron hub, translocating reducing equivalents from cytoplasmic thioredoxin to a number of periplasmic substrates involved in oxidative protein folding, cytochrome c maturation and oxidative stress defence. DsbD is a multi-domain protein consisting of a transmembrane domain (t-DsbD) flanked by two periplasmic domains (n-DsbD and c-DsbD). Previous studies have shown that DsbD is required for the survival of the obligate human pathogen Neisseria meningitidis. To help understand the structural and functional aspects of N. meningitidis DsbD, the two periplasmic domains which are required for electron transfer are being studied. Here, the expression, purification and biophysical properties of n-NmDsbD and c-NmDsbD are described. The crystallization and crystallographic analysis of n-NmDsbD and c-NmDsbD are also described in both redox states, which differ only in the presence or absence of a disulfide bond but which crystallized in completely different conditions. Crystals of n-NmDsbDOx, n-NmDsbDRed, c-NmDsbDOx and c-NmDsbDRed diffracted to 2.3, 1.6, 2.3 and 1.7 A resolution and belonged to space groups P213, P321, P41 and P1211, respectively. | |||
Production, biophysical characterization and initial crystallization studies of the N- and C-terminal domains of DsbD, an essential enzyme in Neisseria meningitidis.,Smith RP, Whitten AE, Paxman JJ, Kahler CM, Scanlon MJ, Heras B Acta Crystallogr F Struct Biol Commun. 2018 Jan 1;74(Pt 1):31-38. doi:, 10.1107/S2053230X17017800. Epub 2018 Jan 1. PMID:29372905<ref>PMID:29372905</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 6dnu" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Protein-disulfide reductase]] | |||
[[Category: Heras, B]] | [[Category: Heras, B]] | ||
[[Category: Smith, R | [[Category: Paxman, J J]] | ||
[[Category: | [[Category: Smith, R P]] | ||
[[Category: Disulphide reductase]] | |||
[[Category: Dsb protein]] | |||
[[Category: Oxidoreductase]] | |||
Revision as of 10:36, 12 September 2018
Crystal Structure of Neisseria meningitidis DsbD c-terminal domain in the oxidised formCrystal Structure of Neisseria meningitidis DsbD c-terminal domain in the oxidised form
Structural highlights
Function[C6S7X6_NEIML] 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. This transfer involves a cascade of disulfide bond formation and reduction steps.[HAMAP-Rule:MF_00399] Publication Abstract from PubMedThe membrane protein DsbD is a reductase that acts as an electron hub, translocating reducing equivalents from cytoplasmic thioredoxin to a number of periplasmic substrates involved in oxidative protein folding, cytochrome c maturation and oxidative stress defence. DsbD is a multi-domain protein consisting of a transmembrane domain (t-DsbD) flanked by two periplasmic domains (n-DsbD and c-DsbD). Previous studies have shown that DsbD is required for the survival of the obligate human pathogen Neisseria meningitidis. To help understand the structural and functional aspects of N. meningitidis DsbD, the two periplasmic domains which are required for electron transfer are being studied. Here, the expression, purification and biophysical properties of n-NmDsbD and c-NmDsbD are described. The crystallization and crystallographic analysis of n-NmDsbD and c-NmDsbD are also described in both redox states, which differ only in the presence or absence of a disulfide bond but which crystallized in completely different conditions. Crystals of n-NmDsbDOx, n-NmDsbDRed, c-NmDsbDOx and c-NmDsbDRed diffracted to 2.3, 1.6, 2.3 and 1.7 A resolution and belonged to space groups P213, P321, P41 and P1211, respectively. Production, biophysical characterization and initial crystallization studies of the N- and C-terminal domains of DsbD, an essential enzyme in Neisseria meningitidis.,Smith RP, Whitten AE, Paxman JJ, Kahler CM, Scanlon MJ, Heras B Acta Crystallogr F Struct Biol Commun. 2018 Jan 1;74(Pt 1):31-38. doi:, 10.1107/S2053230X17017800. Epub 2018 Jan 1. PMID:29372905[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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