2k0r: Difference between revisions

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{{Seed}}
[[Image:2k0r.jpg|left|200px]]


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==Solution structure of the C103S mutant of the N-terminal Domain of DsbD from Neisseria meningitidis==
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<StructureSection load='2k0r' size='340' side='right'caption='[[2k0r]]' scene=''>
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== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<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>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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<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>
{{STRUCTURE_2k0r|  PDB=2k0r  |  SCENE=  }}
</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].
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<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 of the C103S mutant of the N-terminal Domain of DsbD from Neisseria meningitidis===
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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 2k0r" style="background-color:#fffaf0;"></div>


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==See Also==
The line below this paragraph, {{ABSTRACT_PUBMED_18983169}}, adds the Publication Abstract to the page
*[[Thiol:disulfide interchange protein 3D structures|Thiol:disulfide interchange protein 3D structures]]
(as it appears on PubMed at http://www.pubmed.gov), where 18983169 is the PubMed ID number.
== References ==
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<references/>
{{ABSTRACT_PUBMED_18983169}}
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</StructureSection>
==About this Structure==
[[Category: Large Structures]]
2K0R is a 1 chain structure of sequence from [http://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].
[[Category: Neisseria meningitidis serogroup B]]
 
[[Category: Averlant-Petit M]]
==Reference==
[[Category: Beaufils C]]
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:[http://www.ncbi.nlm.nih.gov/pubmed/18983169 18983169]
[[Category: Boschi-Muller S]]
[[Category: Neisseria meningitidis serogroup b]]
[[Category: Branlant G]]
[[Category: Protein-disulfide reductase]]
[[Category: Cung M]]
[[Category: Averlant-Petit, M.]]
[[Category: Jacob C]]
[[Category: Beaufils, C.]]
[[Category: Quinternet M]]
[[Category: Boschi-Muller, S.]]
[[Category: Selme L]]
[[Category: Branlant, G.]]
[[Category: Tsan P]]
[[Category: Cung, M.]]
[[Category: Jacob, C.]]
[[Category: Quinternet, M.]]
[[Category: Selme, L.]]
[[Category: Tsan, P.]]
[[Category: Cytochrome c-type biogenesis]]
[[Category: Disulfide bond reductase]]
[[Category: Electron transport]]
[[Category: Immunoglobulin]]
[[Category: Inner membrane]]
[[Category: Membrane]]
[[Category: Mutant]]
[[Category: N-terminal domain]]
[[Category: Nad]]
[[Category: Oxidoreductase]]
[[Category: Redox-active center]]
[[Category: Transmembrane]]
[[Category: Transport]]
 
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