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1uyn

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Revision as of 08:14, 28 March 2018

Translocator domain of autotransporter NalP from Neisseria meningitidis

Structural highlights

1uyn is a 1 chain structure with sequence from "diplokokkus_intracellularis_meningitidis"_(sic)_weichselbaum_1887 "diplokokkus intracellularis meningitidis" (sic) weichselbaum 1887. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Related:	1uyo
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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

Autotransporters are virulence-related proteins of Gram-negative bacteria that are secreted via an outer-membrane-based C-terminal extension, the translocator domain. This domain supposedly is sufficient for the transport of the N-terminal passenger domain across the outer membrane. We present here the crystal structure of the in vitro-folded translocator domain of the autotransporter NalP from Neisseria meningitidis, which reveals a 12-stranded beta-barrel with a hydrophilic pore of 10 x 12.5 A that is filled by an N-terminal alpha-helix. The domain has pore activity in vivo and in vitro. Our data are consistent with the model of passenger-domain transport through the hydrophilic channel within the beta-barrel, and inconsistent with a model for transport through a central channel formed by an oligomer of translocator domains. However, the dimensions of the pore imply translocation of the secreted domain in an unfolded form. An alternative model, possibly covering the transport of folded domains, is that passenger-domain transport involves the Omp85 complex, the machinery required for membrane insertion of outer-membrane proteins, on which autotransporters are dependent.

Structure of the translocator domain of a bacterial autotransporter.,Oomen CJ, van Ulsen P, van Gelder P, Feijen M, Tommassen J, Gros P EMBO J. 2004 Mar 24;23(6):1257-66. Epub 2004 Mar 11. PMID:15014442^[1]

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

References

↑ Oomen CJ, van Ulsen P, van Gelder P, Feijen M, Tommassen J, Gros P. Structure of the translocator domain of a bacterial autotransporter. EMBO J. 2004 Mar 24;23(6):1257-66. Epub 2004 Mar 11. PMID:15014442 doi:http://dx.doi.org/10.1038/sj.emboj.7600148

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1uyn"

@@ Line 1: / Line 1: @@
-==TRANSLOCATOR DOMAIN OF AUTOTRANSPORTER NALP FROM NEISSERIA MENINGITIDIS==
+==Translocator domain of autotransporter NalP from Neisseria meningitidis==
 <StructureSection load='1uyn' size='340' side='right' caption='[[1uyn]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
 == Structural highlights ==
@@ Line 5: / Line 6: @@
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CXE:PENTAETHYLENE+GLYCOL+MONODECYL+ETHER'>CXE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1uyo|1uyo]]</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=1uyn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1uyn OCA], [http://pdbe.org/1uyn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1uyn RCSB], [http://www.ebi.ac.uk/pdbsum/1uyn 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=1uyn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1uyn OCA], [http://pdbe.org/1uyn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1uyn RCSB], [http://www.ebi.ac.uk/pdbsum/1uyn PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1uyn ProSAT]</span></td></tr>
 </table>
 == Evolutionary Conservation ==
@@ Line 11: / Line 12: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/uy/1uyn_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/uy/1uyn_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
@@ Line 28: / Line 29: @@
 ==See Also==
-*[[Translocator Domain of the Autotransporter NalP within Neisseria meningitidis|Translocator Domain of the Autotransporter NalP within Neisseria meningitidis]]
+*[[NalP|NalP]]
 == References ==
 <references/>

1uyn

From Proteopedia

Revision as of 08:14, 28 March 2018

Translocator domain of autotransporter NalP from Neisseria meningitidis

Structural highlights

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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