3gea
From Proteopedia
(Difference between revisions)
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- | + | ==Donor strand complemented FaeG monomer of F4 variant ad== | |
- | + | <StructureSection load='3gea' size='340' side='right' caption='[[3gea]], [[Resolution|resolution]] 1.70Å' scene=''> | |
- | + | == Structural highlights == | |
- | + | <table><tr><td colspan='2'>[[3gea]] 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=3GEA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3GEA FirstGlance]. <br> | |
- | ==Function== | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</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">[[2j6g|2j6g]], [[2j6r|2j6r]], [[3f65|3f65]], [[3gew|3gew]], [[3gfu|3gfu]], [[3ggh|3ggh]], [[3hlr|3hlr]]</td></tr> | ||
+ | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">faeG ([http://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=3gea FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3gea OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3gea RCSB], [http://www.ebi.ac.uk/pdbsum/3gea PDBsum]</span></td></tr> | ||
+ | </table> | ||
+ | == Function == | ||
[[http://www.uniprot.org/uniprot/FAEG3_ECOLX FAEG3_ECOLX]] K88 major fimbrial subunit. Fimbriae (also called pili), are polar filaments radiating from the surface of the bacterium to a length of 0.5-1.5 micrometers and numbering 100-300 per cell. They enable bacteria to colonize the epithelium of specific host organs. | [[http://www.uniprot.org/uniprot/FAEG3_ECOLX FAEG3_ECOLX]] K88 major fimbrial subunit. Fimbriae (also called pili), are polar filaments radiating from the surface of the bacterium to a length of 0.5-1.5 micrometers and numbering 100-300 per cell. They enable bacteria to colonize the epithelium of specific host organs. | ||
+ | == Evolutionary Conservation == | ||
+ | [[Image:Consurf_key_small.gif|200px|right]] | ||
+ | Check<jmol> | ||
+ | <jmolCheckbox> | ||
+ | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ge/3gea_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]. | ||
+ | <div style="clear:both"></div> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | Enterotoxigenic Escherichia coli expressing F4 fimbriae are the major cause of porcine colibacillosis and are responsible for significant death and morbidity in neonatal and postweaned piglets. Via the chaperone-usher pathway, F4 fimbriae are assembled into thin, flexible polymers mainly composed of the single-domain adhesin FaeG. The F4 fimbrial system has been labeled eccentric because the F4 pilins show some features distinct from the features of pilins of other chaperone-usher-assembled structures. In particular, FaeG is much larger than other pilins (27 versus approximately 17 kDa), grafting an additional carbohydrate binding domain on the common immunoglobulin-like core. Structural data of FaeG during different stages of the F4 fimbrial biogenesis process, combined with differential scanning calorimetry measurements, confirm the general principles of the donor strand complementation/exchange mechanisms taking place during pilus biogenesis via the chaperone-usher pathway. | ||
- | + | Structural and thermodynamic characterization of pre- and postpolymerization states in the F4 fimbrial subunit FaeG.,Van Molle I, Moonens K, Garcia-Pino A, Buts L, De Kerpel M, Wyns L, Bouckaert J, De Greve H J Mol Biol. 2009 Dec 18;394(5):957-67. Epub 2009 Sep 30. PMID:19799915<ref>PMID:19799915</ref> | |
- | + | ||
+ | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
+ | </div> | ||
==See Also== | ==See Also== | ||
*[[Pilin|Pilin]] | *[[Pilin|Pilin]] | ||
- | + | == References == | |
- | == | + | <references/> |
- | + | __TOC__ | |
+ | </StructureSection> | ||
[[Category: Bacillus coli migula 1895]] | [[Category: Bacillus coli migula 1895]] | ||
- | [[Category: Bouckaert, J | + | [[Category: Bouckaert, J]] |
- | [[Category: Buts, L | + | [[Category: Buts, L]] |
- | [[Category: Garcia-Pino, A | + | [[Category: Garcia-Pino, A]] |
- | [[Category: Greve, H De | + | [[Category: Greve, H De]] |
- | [[Category: Molle, I Van | + | [[Category: Molle, I Van]] |
- | [[Category: Moonens, K | + | [[Category: Moonens, K]] |
[[Category: Cell adhesion]] | [[Category: Cell adhesion]] | ||
[[Category: Fimbrium]] | [[Category: Fimbrium]] | ||
[[Category: Immunoglobulin like fold]] | [[Category: Immunoglobulin like fold]] |
Revision as of 01:59, 25 December 2014
Donor strand complemented FaeG monomer of F4 variant ad
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