2k9f: Difference between revisions
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[[Image: | ==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 [http://en.wikipedia.org/wiki/Neisseria_meningitidis_serogroup_a Neisseria meningitidis serogroup a] and [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=2K9F OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2K9F FirstGlance]. <br> | |||
</td></tr><tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2k0r|2k0r]], [[2jzs|2jzs]]</td></tr> | |||
<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">msrAB, pilB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=65699 Neisseria meningitidis serogroup A]), dsbD ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=491 Neisseria meningitidis serogroup B])</td></tr> | |||
<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Protein-disulfide_reductase Protein-disulfide reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.1.8 1.8.1.8] </span></td></tr> | |||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2k9f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2k9f OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2k9f RCSB], [http://www.ebi.ac.uk/pdbsum/2k9f PDBsum]</span></td></tr> | |||
<table> | |||
== 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/chain_selection.php?pdb_ID=2ata 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> | |||
==See Also== | ==See Also== | ||
*[[Thioredoxin|Thioredoxin]] | *[[Thioredoxin|Thioredoxin]] | ||
== References == | |||
== | <references/> | ||
< | __TOC__ | ||
</StructureSection> | |||
[[Category: Neisseria meningitidis serogroup a]] | [[Category: Neisseria meningitidis serogroup a]] | ||
[[Category: Neisseria meningitidis serogroup b]] | [[Category: Neisseria meningitidis serogroup b]] | ||
Revision as of 05:33, 29 September 2014
Structural features of the complex between the DsbD N-terminal and the PilB N-terminal domains from Neisseria meningitidis
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Proteopedia Page Contributors and Editors (what is this?)
Categories:
- Neisseria meningitidis serogroup a
- Neisseria meningitidis serogroup b
- 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
