2k9f
From Proteopedia
(Difference between revisions)
(5 intermediate revisions not shown.) | |||
Line 1: | Line 1: | ||
- | [[Image:2k9f.png|left|200px]] | ||
- | + | ==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. | ||
- | + | 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> | |
- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | + | </div> | |
- | + | <div class="pdbe-citations 2k9f" style="background-color:#fffaf0;"></div> | |
- | + | ||
==See Also== | ==See Also== | ||
- | *[[Thioredoxin|Thioredoxin]] | + | *[[Thiol:disulfide interchange protein 3D structures|Thiol:disulfide interchange protein 3D structures]] |
- | + | *[[Thioredoxin 3D structures|Thioredoxin 3D structures]] | |
- | == | + | == References == |
- | < | + | <references/> |
- | [[Category: | + | __TOC__ |
- | [[Category: Neisseria meningitidis serogroup | + | </StructureSection> |
- | [[Category: | + | [[Category: Large Structures]] |
- | [[Category: Boschi-Muller | + | [[Category: Neisseria meningitidis serogroup A]] |
- | [[Category: Branlant | + | [[Category: Neisseria meningitidis serogroup B]] |
- | [[Category: Cung | + | [[Category: Boschi-Muller S]] |
- | [[Category: Jacob | + | [[Category: Branlant G]] |
- | [[Category: Quinternet | + | [[Category: Cung M]] |
- | [[Category: Selme | + | [[Category: Jacob C]] |
- | [[Category: Tsan | + | [[Category: Quinternet M]] |
- | + | [[Category: Selme L]] | |
- | + | [[Category: Tsan P]] | |
- | + | ||
- | + | ||
- | + | ||
- | + | ||
- | + | ||
- | + | ||
- | + | ||
- | + | ||
- | + | ||
- | + | ||
- | + | ||
- | + | ||
- | + | ||
- | + |
Current revision
Structural features of the complex between the DsbD N-terminal and the PilB N-terminal domains from Neisseria meningitidis
|