3hlr: Difference between revisions

From Proteopedia
Jump to navigationJump to search
OCA (talk | contribs)
No edit summary
OCA (talk | contribs)
No edit summary
Line 1: Line 1:
{{STRUCTURE_3hlr| PDB=3hlr | SCENE= }}
==Donor strand complemented FaeG of F4ad fimbriae==
===Donor strand complemented FaeG of F4ad fimbriae===
<StructureSection load='3hlr' size='340' side='right' caption='[[3hlr]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
{{ABSTRACT_PUBMED_19799915}}
== Structural highlights ==
<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://www.rcsb.org/pdb/explore.do?structureId=3hlr RCSB], [http://www.ebi.ac.uk/pdbsum/3hlr 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.
== 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/hl/3hlr_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.


==Function==
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>
[[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.  


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[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].
</div>


==See Also==
==See Also==
*[[Pilin|Pilin]]
*[[Pilin|Pilin]]
 
== References ==
==Reference==
<references/>
<ref group="xtra">PMID:019799915</ref><references group="xtra"/><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: Immunoglobuline like fold]]
[[Category: Immunoglobuline like fold]]