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==Crystal Structure of Neisseria meningitidis DsbD c-terminal domain in the reduced form==
==Crystal Structure of Neisseria meningitidis DsbD c-terminal domain in the reduced form==
<StructureSection load='6dnl' size='340' side='right' caption='[[6dnl]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
<StructureSection load='6dnl' size='340' side='right'caption='[[6dnl]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[6dnl]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6DNL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6DNL FirstGlance]. <br>
<table><tr><td colspan='2'>[[6dnl]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Neisseria_meningitidis Neisseria meningitidis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6DNL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6DNL FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7&#8491;</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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=6dnl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6dnl OCA], [http://pdbe.org/6dnl PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6dnl RCSB], [http://www.ebi.ac.uk/pdbsum/6dnl PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6dnl ProSAT]</span></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=6dnl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6dnl OCA], [https://pdbe.org/6dnl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6dnl RCSB], [https://www.ebi.ac.uk/pdbsum/6dnl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6dnl ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/A0A0Y6T358_NEIME A0A0Y6T358_NEIME]] 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]
[https://www.uniprot.org/uniprot/DSBD_NEIMB DSBD_NEIMB] 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 (By similarity).
<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>
==See Also==
 
*[[Thiol:disulfide interchange protein 3D structures|Thiol:disulfide interchange protein 3D structures]]
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6dnl" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Protein-disulfide reductase]]
[[Category: Large Structures]]
[[Category: Heras, B]]
[[Category: Neisseria meningitidis]]
[[Category: Paxman, J J]]
[[Category: Heras B]]
[[Category: Smith, R P]]
[[Category: Paxman JJ]]
[[Category: Disulphide reductase]]
[[Category: Smith RP]]
[[Category: Dsb protein]]
[[Category: Oxidoreductase]]

Latest revision as of 14:36, 13 March 2024

Crystal Structure of Neisseria meningitidis DsbD c-terminal domain in the reduced form

6dnl, resolution 1.70Å

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