3fip: Difference between revisions

← Older edit

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 3: / Line 3: @@
 <StructureSection load='3fip' size='340' side='right'caption='[[3fip]], [[Resolution|resolution]] 3.15&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3fip]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3FIP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3FIP FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3fip]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3FIP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3FIP 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;'>[[2vqi|2vqi]]</div></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]] 3.154&#8491;</td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Escherichia coli Enterobacteriaceae, papC ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</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=3fip FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fip OCA], [https://pdbe.org/3fip PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3fip RCSB], [https://www.ebi.ac.uk/pdbsum/3fip PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3fip ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/PAPC_ECOLX PAPC_ECOLX]] Involved in the export and assembly of pili subunits across the outer membrane. Forms a hexameric ring-shaped pore in the outer bacterial membrane. The 2 nanometer-diameter pore allows the passage of the thin tip fibrillum. As for the rod, it probably unwinds into linear fibers which would therefore be narrow enough to pass through the pore.
+[https://www.uniprot.org/uniprot/PAPC_ECOLX PAPC_ECOLX] Involved in the export and assembly of pili subunits across the outer membrane. Forms a hexameric ring-shaped pore in the outer bacterial membrane. The 2 nanometer-diameter pore allows the passage of the thin tip fibrillum. As for the rod, it probably unwinds into linear fibers which would therefore be narrow enough to pass through the pore.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 20: / Line 19: @@
 </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=3fip ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-Ushers constitute a family of bacterial outer membrane proteins responsible for the assembly and secretion of surface organelles such as the pilus. The structure at 3.15-A resolution of the usher pyelonephritis-associated pili C (PapC) translocation domain reveals a 24-stranded kidney-shaped beta-barrel, occluded by an internal plug domain. The dimension of the pore allows tandem passage of individual folded pilus subunits in an upright pilus growth orientation, but is insufficient for accommodating donor strand exchange. The molecular packing revealed by the crystal structure shows that 2 PapC molecules in head-to-head orientation interact via exposed beta-strand edges, which could be the preferred dimer interaction in solution. In vitro reconstitution of fiber assemblies suggest that PapC monomers may be sufficient for fiber assembly and secretion; both the plug domain and the C-terminal domain of PapC are required for filament assembly, whereas the N-terminal domain is mainly responsible for recruiting the chaperone-subunit complexes to the usher. The plug domain has a dual function: gating the beta-pore and participating in pilus assembly.
-Insights into pilus assembly and secretion from the structure and functional characterization of usher PapC.,Huang Y, Smith BS, Chen LX, Baxter RH, Deisenhofer J Proc Natl Acad Sci U S A. 2009 May 5;106(18):7403-7. Epub 2009 Apr 20. PMID:19380723<ref>PMID:19380723</ref>
+==See Also==
+*[[Adhesin 3D structures|Adhesin 3D structures]]
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 3fip" style="background-color:#fffaf0;"></div>
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: Bacillus coli migula 1895]]
+[[Category: Escherichia coli]]
 [[Category: Large Structures]]
-[[Category: Deisenhofer, J]]
+[[Category: Deisenhofer J]]
-[[Category: Huang, Y]]
+[[Category: Huang Y]]
-[[Category: Beta barrel]]
-[[Category: Cell membrane]]
-[[Category: Cell outer membrane]]
-[[Category: Fimbrium]]
-[[Category: Membrane]]
-[[Category: Protein translocase]]
-[[Category: Transmembrane]]
-[[Category: Transport]]
-[[Category: Transport protein]]