2k0r: Difference between revisions
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New page: '''Unreleased structure''' The entry 2k0r is ON HOLD Authors: Quinternet, M., Selme, L., Tsan, P., Beaufils, C., Jacob, C., Boschi-Muller, S., Averlant-Petit, M., Branlant, G., Cung, M.... |
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The | ==Solution structure of the C103S mutant of the N-terminal Domain of DsbD from Neisseria meningitidis== | ||
<StructureSection load='2k0r' size='340' side='right'caption='[[2k0r]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2k0r]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Neisseria_meningitidis_serogroup_B Neisseria meningitidis serogroup B]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2K0R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2K0R FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=2k0r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2k0r OCA], [https://pdbe.org/2k0r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2k0r RCSB], [https://www.ebi.ac.uk/pdbsum/2k0r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2k0r ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[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). | |||
== 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/k0/2k0r_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/main_output.php?pdb_ID=2k0r ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The DsbD protein is essential for electron transfer from the cytoplasm to the periplasm of Gram-negative bacteria. Its N-terminal domain dispatches electrons coming from cytoplasmic thioredoxin (Trx), via its central transmembrane and C-terminal domains, to its periplasmic partners: DsbC, DsbE/CcmG, and DsbG. Previous structural studies described the latter proteins as Trx-like folds possessing a characteristic C-X-X-C motif able to generate a disulfide bond upon oxidation. The Escherichia coli nDsbD displays an immunoglobulin-like fold in which two cysteine residues (Cys103 and Cys109) allow a disulfide bond exchange with its biological partners.We have determined the structure in solution and the backbone dynamics of the C103S mutant of the N-terminal domain of DsbD from Neisseria meningitidis. Our results highlight significant structural changes concerning the beta-sheets and the local topology of the active site compared with the oxidized form of the E. coli nDsbD. The structure reveals a "cap loop" covering the active site, similar to the oxidized E. coli nDsbD X-ray structure. However, regions featuring enhanced mobility were observed both near to and distant from the active site, revealing a capacity of structural adjustments in the active site and in putative interaction areas with nDsbD biological partners. Results are discussed in terms of functional consequences. | |||
Solution Structure and Backbone Dynamics of the Cysteine 103 to Serine Mutant of the N-Terminal Domain of DsbD from Neisseria meningitides.,Quinternet M, Tsan P, Selme L, Beaufils C, Jacob C, Boschi-Muller S, Averlant-Petit MC, Branlant G, Cung MT Biochemistry. 2008 Nov 5. PMID:18983169<ref>PMID:18983169</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2k0r" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Thiol:disulfide interchange protein 3D structures|Thiol:disulfide interchange protein 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Neisseria meningitidis serogroup B]] | |||
[[Category: Averlant-Petit M]] | |||
[[Category: Beaufils C]] | |||
[[Category: Boschi-Muller S]] | |||
[[Category: Branlant G]] | |||
[[Category: Cung M]] | |||
[[Category: Jacob C]] | |||
[[Category: Quinternet M]] | |||
[[Category: Selme L]] | |||
[[Category: Tsan P]] | |||
