1qun

<table><tr><td colspan='2'>[[1qun]] is a 16 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=1QUN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QUN FirstGlance]. <br>

</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=1qun FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qun OCA], [https://pdbe.org/1qun PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qun RCSB], [https://www.ebi.ac.uk/pdbsum/1qun PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qun ProSAT]</span></td></tr>

[[https://www.uniprot.org/uniprot/FIMC_ECOLI FIMC_ECOLI]] Required for the biogenesis of type 1 fimbriae. Binds and interact with FimH. [[https://www.uniprot.org/uniprot/FIMH_ECOLI FIMH_ECOLI]] Involved in regulation of length and mediation of adhesion of type 1 fimbriae (but not necessary for the production of fimbriae). Adhesin responsible for the binding to D-mannose. It is laterally positioned at intervals in the structure of the type 1 fimbriae. In order to integrate FimH in the fimbriae FimF and FimG are needed.

<div style="background-color:#fffaf0;">

== Publication Abstract from PubMed ==

Type 1 pili-adhesive fibers expressed in most members of the Enterobacteriaceae family-mediate binding to mannose receptors on host cells through the FimH adhesin. Pilus biogenesis proceeds by way of the chaperone/usher pathway. The x-ray structure of the FimC-FimH chaperone-adhesin complex from uropathogenic Escherichia coli at 2.5 angstrom resolution reveals the basis for carbohydrate recognition and for pilus assembly. The carboxyl-terminal pilin domain of FimH has an immunoglobulin-like fold, except that the seventh strand is missing, leaving part of the hydrophobic core exposed. A donor strand complementation mechanism in which the chaperone donates a strand to complete the pilin domain explains the basis for both chaperone function and pilus biogenesis.

X-ray structure of the FimC-FimH chaperone-adhesin complex from uropathogenic Escherichia coli.,Choudhury D, Thompson A, Stojanoff V, Langermann S, Pinkner J, Hultgren SJ, Knight SD Science. 1999 Aug 13;285(5430):1061-6. PMID:10446051<ref>PMID:10446051</ref>

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

</div>

<div class="pdbe-citations 1qun" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Bacillus coli migula 1895]]

[[Category: Choudhury, D]]

[[Category: Hultgren, S J]]

[[Category: Knight, S]]

[[Category: Langerman, S]]

[[Category: Pinkner, J]]

[[Category: Stojanoff, V]]

[[Category: Thompson, A]]

[[Category: Chaperone-structural protein complex]]