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==Crystal structure of para-biphenyl-2-methyl-3'-methyl amide mannoside bound to FimH lectin domain== | ==Crystal structure of para-biphenyl-2-methyl-3'-methyl amide mannoside bound to FimH lectin domain== | ||
<StructureSection load='5f3f' size='340' side='right' caption='[[5f3f]], [[Resolution|resolution]] 1.76Å' scene=''> | <StructureSection load='5f3f' size='340' side='right'caption='[[5f3f]], [[Resolution|resolution]] 1.76Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5f3f]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5F3F OCA]. For a <b>guided tour on the structure components</b> use [http:// | <table><tr><td colspan='2'>[[5f3f]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli_j96 Escherichia coli j96]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5F3F OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5F3F FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=5US:3-[4-[(2~{R},3~{S},4~{S},5~{S},6~{R})-6-(HYDROXYMETHYL)-3,4,5-TRIS(OXIDANYL)OXAN-2-YL]OXY-3-METHYL-PHENYL]-~{N}-METHYL-BENZAMIDE'>5US</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=5US:3-[4-[(2~{R},3~{S},4~{S},5~{S},6~{R})-6-(HYDROXYMETHYL)-3,4,5-TRIS(OXIDANYL)OXAN-2-YL]OXY-3-METHYL-PHENYL]-~{N}-METHYL-BENZAMIDE'>5US</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5f2f|5f2f]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5f2f|5f2f]]</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http:// | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">fimH ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1206108 Escherichia coli J96])</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5f3f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5f3f OCA], [http://pdbe.org/5f3f PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5f3f RCSB], [http://www.ebi.ac.uk/pdbsum/5f3f PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5f3f ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | == Function == | ||
[[http://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. | [[http://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. | ||
==See Also== | |||
*[[Adhesin 3D structures|Adhesin 3D structures]] | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Escherichia coli j96]] | |||
[[Category: Large Structures]] | |||
[[Category: Hultgren, S J]] | [[Category: Hultgren, S J]] | ||
[[Category: Klein, R D]] | [[Category: Klein, R D]] | ||
Revision as of 10:57, 29 April 2020
Crystal structure of para-biphenyl-2-methyl-3'-methyl amide mannoside bound to FimH lectin domainCrystal structure of para-biphenyl-2-methyl-3'-methyl amide mannoside bound to FimH lectin domain
Structural highlights
Function[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. See Also |
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