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2k9f
From Proteopedia
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| - | {{Seed}} | ||
| - | [[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]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[2k9f]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Neimd Neimd] and [https://en.wikipedia.org/wiki/Neimi Neimi]. 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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2k0r|2k0r]], [[2jzs|2jzs]]</div></td></tr> | |
| - | - | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">msrAB, pilB ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=65699 NEIMD]), dsbD ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=491 NEIMI])</td></tr> |
| - | + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Protein-disulfide_reductase Protein-disulfide reductase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.1.8 1.8.1.8] </span></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. [[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/k9/2k9f_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=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== | |
| - | + | *[[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: Neimd]] | |
| - | == | + | [[Category: Neimi]] |
| - | < | + | |
| - | [[Category: | + | |
| - | [[Category: | + | |
[[Category: Protein-disulfide reductase]] | [[Category: Protein-disulfide reductase]] | ||
| - | [[Category: Boschi-Muller, S | + | [[Category: Boschi-Muller, S]] |
| - | [[Category: Branlant, G | + | [[Category: Branlant, G]] |
| - | [[Category: Cung, M | + | [[Category: Cung, M]] |
| - | [[Category: Jacob, C | + | [[Category: Jacob, C]] |
| - | [[Category: Quinternet, M | + | [[Category: Quinternet, M]] |
| - | [[Category: Selme, L | + | [[Category: Selme, L]] |
| - | [[Category: Tsan, P | + | [[Category: Tsan, P]] |
[[Category: Cytochrome c-type biogenesis]] | [[Category: Cytochrome c-type biogenesis]] | ||
[[Category: Docking]] | [[Category: Docking]] | ||
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[[Category: Transmembrane]] | [[Category: Transmembrane]] | ||
[[Category: Transport]] | [[Category: Transport]] | ||
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| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Sep 3 15:59:40 2009'' | ||
Current revision
Structural features of the complex between the DsbD N-terminal and the PilB N-terminal domains from Neisseria meningitidis
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Categories: Large Structures | Neimd | Neimi | Protein-disulfide reductase | Boschi-Muller, S | Branlant, G | Cung, M | Jacob, C | Quinternet, M | Selme, L | Tsan, P | Cytochrome c-type biogenesis | Docking | Dsbd | Electron transport | Immunoglobulin | Inner membrane | Membrane | Multifunctional enzyme | Nad | Oxidoreductase | Pilb | Protein | Redox-active center | Thioredoxin | Transmembrane | Transport

