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==TRANSLOCATOR DOMAIN OF AUTOTRANSPORTER NALP FROM NEISSERIA MENINGITIDIS==
 
<StructureSection load='1uyn' size='340' side='right' caption='[[1uyn]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
==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 ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1uyn]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"diplokokkus_intracellularis_meningitidis"_(sic)_weichselbaum_1887 "diplokokkus intracellularis meningitidis" (sic) weichselbaum 1887]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UYN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1UYN FirstGlance]. <br>
<table><tr><td colspan='2'>[[1uyn]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Neisseria_meningitidis Neisseria meningitidis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UYN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1UYN FirstGlance]. <br>
</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>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1uyo|1uyo]]</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CXE:PENTAETHYLENE+GLYCOL+MONODECYL+ETHER'>CXE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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'>[https://proteopedia.org/fgij/fg.htm?mol=1uyn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1uyn OCA], [https://pdbe.org/1uyn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1uyn RCSB], [https://www.ebi.ac.uk/pdbsum/1uyn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1uyn ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/NALP_NEIMH NALP_NEIMH] Major human immunogenic protein. Autotransporter with a secreted protease domain involved in processing other autotransporter proteins including App and IgA. Probably autoprocesses to release the about 70 kDa passenger domain (PubMed:14617158). Processes the lactoferrin receptor lipoprotein subunit (LbpB) extracellularly, releasing it from the cell surface. LbpB release protects bacteria against complement-mediated killing by anti-LbpB antibodies (PubMed:20421383). Processes NHBA (PubMed:23258267). Lipidation slows its auto-processing, probably allowing it to act on endogenous substrates on the cell suface before the passenger domain is released into the medium (PubMed:23258267). The C-terminal beta-barrel domain inserts into the outer membrane where it probably exports the N-terminal passenger domain (PubMed:15014442). Both the cell surface protein (Neisserial autotransporter lipoprotein NalP) and the passenger domain cleave human (host) complement factor C3, generating a shorter alpha chain and a longer beta chain than normal (By similarity).[UniProtKB:Q9JXM7]<ref>PMID:14617158</ref> <ref>PMID:15014442</ref> <ref>PMID:20421383</ref> <ref>PMID:23258267</ref>  Plays a role in extracellular-DNA (eDNA) mediated biofilm formation. In some strains (including cc32 strain H44/76 but not cc11 strain B16B6) eDNA stimulates biofilm formation. When NalP is not expressed (and no longer processes NHBA or IgA) biofilm formation increases (PubMed:23163582). This is probably because the number of positively charged, DNA-binding peptides on the cell surface rises, resulting in increased biofilm formation (Probable).<ref>PMID:23163582</ref> <ref>PMID:23163582</ref>  Cleaves human (host) complement factor C3, generating a shorter alpha chain and a longer beta chain than normal. Does not act on mouse or rabbit C3. Cleavage causes C3b degradation by human CFI and CFH, decreases deposition of C3b on the bacteria surface and probably facilitates complement escape.[UniProtKB:Q9JXM7]
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
   <jmolCheckbox>
   <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>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
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==See Also==
==See Also==
*[[Translocator Domain of the Autotransporter NalP within Neisseria meningitidis|Translocator Domain of the Autotransporter NalP within Neisseria meningitidis]]
*[[NalP|NalP]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Feijen, M]]
[[Category: Large Structures]]
[[Category: Gelder, P Van]]
[[Category: Neisseria meningitidis]]
[[Category: Gros, P]]
[[Category: Feijen M]]
[[Category: Oomen, C J]]
[[Category: Gros P]]
[[Category: Tommassen, J]]
[[Category: Oomen CJ]]
[[Category: Ulsen, P Van]]
[[Category: Tommassen J]]
[[Category: Autotransporter]]
[[Category: Van Gelder P]]
[[Category: Beta-barrel]]
[[Category: Van Ulsen P]]
[[Category: Beta-domain]]
[[Category: Membrane protein]]
[[Category: Outer membrane]]
[[Category: Translocator domain]]

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