2k9f: Difference between revisions

<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>

[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.

    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/k9/2k9f_consurf.spt"</scriptWhenChecked>

    <text>to colour the structure by Evolutionary Conservation</text>

</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].

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.

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>

==See Also==

*[[Thiol:disulfide interchange protein 3D structures|Thiol:disulfide interchange protein 3D structures]]

*[[Thioredoxin 3D structures|Thioredoxin 3D structures]]

== References ==

<references/>

</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]]