3hlr

<StructureSection load='3hlr' size='340' side='right' caption='[[3hlr]], [[Resolution|resolution]] 2.30&Aring;' scene=''>

<table><tr><td colspan='2'>[[3hlr]] is a 1 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=3HLR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3HLR FirstGlance]. <br>

</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3gfu|3gfu]], [[3gew|3gew]], [[3gea|3gea]], [[3ggh|3ggh]], [[2j6g|2j6g]], [[2j6r|2j6r]]</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=3hlr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hlr OCA], [http://pdbe.org/3hlr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3hlr RCSB], [http://www.ebi.ac.uk/pdbsum/3hlr PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3hlr ProSAT]</span></td></tr>

[[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.

<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hl/3hlr_consurf.spt"</scriptWhenChecked>

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== 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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 3hlr" style="background-color:#fffaf0;"></div>

*[[Pilin|Pilin]]

[[Category: Bacillus coli migula 1895]]

[[Category: Bouckaert, J]]

[[Category: Buts, L]]

[[Category: Garcia-Pino, A]]

[[Category: Greve, H De]]

[[Category: Molle, I Van]]

[[Category: Moonens, K]]

[[Category: Cell adhesion]]

[[Category: Immunoglobuline like fold]]