2k9f

From Proteopedia

(Difference between revisions)

Revision as of 10:19, 18 July 2018

Structural features of the complex between the DsbD N-terminal and the PilB N-terminal domains from Neisseria meningitidis

Structural highlights

2k9f is a 2 chain structure with sequence from Neimd and Neimi. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	2k0r, 2jzs
Gene:	msrAB, pilB (NEIMD), dsbD (NEIMI)
Activity:	Protein-disulfide reductase, with EC number 1.8.1.8
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[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. [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

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Quinternet M, Tsan P, Selme-Roussel L, Jacob C, Boschi-Muller S, Branlant G, Cung MT. Formation of the complex between DsbD and PilB N-terminal domains from Neisseria meningitidis necessitates an adaptability of nDsbD. Structure. 2009 Jul 15;17(7):1024-33. PMID:19604482 doi:10.1016/j.str.2009.05.011

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2k9f"

@@ Line 1: / Line 1: @@
 ==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=''>
@@ Line 6: / Line 7: @@
 <tr id='gene'><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 NEIMD]), dsbD ([http://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'>[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 id='resources'><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://pdbe.org/2k9f PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2k9f RCSB], [http://www.ebi.ac.uk/pdbsum/2k9f PDBsum]</span></td></tr>
+<tr id='resources'><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://pdbe.org/2k9f PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2k9f RCSB], [http://www.ebi.ac.uk/pdbsum/2k9f PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2k9f ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 14: / Line 15: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/k9/2k9f_consurf.spt"</scriptWhenChecked>
+    <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].
+</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;">

2k9f

From Proteopedia

Revision as of 10:19, 18 July 2018

Structural features of the complex between the DsbD N-terminal and the PilB N-terminal domains from Neisseria meningitidis

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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