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3fip

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Revision as of 08:02, 2 March 2022

Crystal structure of Usher PapC translocation pore

Structural highlights

3fip is a 2 chain structure with sequence from "bacillus_coli"_migula_1895 "bacillus coli" migula 1895. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	2vqi
Gene:	Escherichia coli Enterobacteriaceae, papC ("Bacillus coli" Migula 1895)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[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

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

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^[1]

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

References

↑ Huang Y, Smith BS, Chen LX, Baxter RH, Deisenhofer J. Insights into pilus assembly and secretion from the structure and functional characterization of usher PapC. Proc Natl Acad Sci U S A. 2009 May 5;106(18):7403-7. Epub 2009 Apr 20. PMID:19380723

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3fip"

@@ Line 1: / Line 1: @@
 ==Crystal structure of Usher PapC translocation pore==
-<StructureSection load='3fip' size='340' side='right' caption='[[3fip]], [[Resolution|resolution]] 3.15&Aring;' scene=''>
+<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 [http://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 [http://oca.weizmann.ac.il/oca-docs/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/"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>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2vqi|2vqi]]</td></tr>
+</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>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Escherichia coli Enterobacteriaceae, papC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3fip FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fip OCA], [http://pdbe.org/3fip PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3fip RCSB], [http://www.ebi.ac.uk/pdbsum/3fip PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3fip ProSAT]</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=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 ==
-[[http://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 34: / Line 34: @@
 </StructureSection>
 [[Category: Bacillus coli migula 1895]]
+[[Category: Large Structures]]
 [[Category: Deisenhofer, J]]
 [[Category: Huang, Y]]

3fip

From Proteopedia

Revision as of 08:02, 2 March 2022

Crystal structure of Usher PapC translocation pore

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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