2k9f: Difference between revisions

New page: '''Unreleased structure''' The entry 2k9f is ON HOLD Authors: Quinternet, M., Tsan, P., Selme, L., Jacob, C., Boschi-Muller, S., Branlant, G., Cung, M. Description: Structural features...
 
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'''Unreleased structure'''


The entry 2k9f is ON HOLD
==Structural features of the complex between the DsbD N-terminal and the PilB N-terminal domains from Neisseria meningitidis==
<StructureSection load='2k9f' size='340' side='right'caption='[[2k9f]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2k9f]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Neisseria_meningitidis_serogroup_A Neisseria meningitidis serogroup A] and [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=2K9F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2K9F FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 10 models</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=2k9f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2k9f OCA], [https://pdbe.org/2k9f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2k9f RCSB], [https://www.ebi.ac.uk/pdbsum/2k9f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2k9f ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/MSRAB_NEIMA MSRAB_NEIMA] Has an important function as a repair enzyme for proteins that have been inactivated by oxidation (By similarity). Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine.
== 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/k9/2k9f_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=2k9f ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
DsbD transmembrane protein dispatches electrons to periplasmic Trx/DsbE-like partners via specific interactions with its N-terminal domain, nDsbD. In the present study, PilB N-terminal domain (NterPilB) is shown to efficiently accept electrons coming from nDsbD from Neisseria meningitidis. Using an NMR-driven docking approach, we have modeled the structure of a mixed disulfide complex between NterPilB and nDsbD. We show the needed opening of nDsbD cap-loop whereas NterPilB FLHE loop does not seem essential in the formation and stabilization of the complex. Relaxation analysis performed on backbone amide groups highlights a kind of dynamics transfer from nDsbD cap-loop on NterPilB alpha1 helix, suggesting that a mobility contribution is required not only for the formation of the mixed disulfide complex, but also for its disruption. Taking into account previous X-ray data on covalent complexes involving nDsbD, a cartoon of interactions between Trx-like partners and nDsbD is proposed that illustrates the adaptability of nDsbD.


Authors: Quinternet, M., Tsan, P., Selme, L., Jacob, C., Boschi-Muller, S., Branlant, G., Cung, M.
Formation of the complex between DsbD and PilB N-terminal domains from Neisseria meningitidis necessitates an adaptability of nDsbD.,Quinternet M, Tsan P, Selme-Roussel L, Jacob C, Boschi-Muller S, Branlant G, Cung MT Structure. 2009 Jul 15;17(7):1024-33. PMID:19604482<ref>PMID:19604482</ref>


Description: Structural features of the complex between the DsbD N-terminal and the PilB N-terminal domains from Neisseria meningitidis
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2k9f" style="background-color:#fffaf0;"></div>


''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Oct 15 13:59:31 2008''
==See Also==
*[[Thiol:disulfide interchange protein 3D structures|Thiol:disulfide interchange protein 3D structures]]
*[[Thioredoxin 3D structures|Thioredoxin 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Neisseria meningitidis serogroup A]]
[[Category: Neisseria meningitidis serogroup B]]
[[Category: Boschi-Muller S]]
[[Category: Branlant G]]
[[Category: Cung M]]
[[Category: Jacob C]]
[[Category: Quinternet M]]
[[Category: Selme L]]
[[Category: Tsan P]]

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