3gew
From Proteopedia
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| - | {{STRUCTURE_3gew| PDB=3gew | SCENE= }} | ||
| - | ===FaeE-FaeG chaperone-major pilin complex of F4 ad fimbriae=== | ||
| - | {{ABSTRACT_PUBMED_19799915}} | ||
| - | == | + | ==FaeE-FaeG chaperone-major pilin complex of F4 ad fimbriae== |
| - | [[3gew]] is a 4 chain structure with sequence from [ | + | <StructureSection load='3gew' size='340' side='right'caption='[[3gew]], [[Resolution|resolution]] 2.00Å' scene=''> |
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[3gew]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3GEW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3GEW FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=3gew FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3gew OCA], [https://pdbe.org/3gew PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3gew RCSB], [https://www.ebi.ac.uk/pdbsum/3gew PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3gew ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/FAEE_ECOLX FAEE_ECOLX] Mediates assembly of pili by forming soluble multimeric complexes with pili subunits as an intermediate step in the assembly process. This protein is involved in K88 pili assembly. Protects pilin protein from proteolytic degradation by DegP and from premature polymerization. | ||
| + | == 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/3gew_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/main_output.php?pdb_ID=3gew 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> |
| + | <div class="pdbe-citations 3gew" style="background-color:#fffaf0;"></div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[Pilin 3D structures|Pilin 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: | + | [[Category: Bouckaert J]] |
| - | [[Category: | + | [[Category: Buts L]] |
| - | [[Category: Greve | + | [[Category: De Greve H]] |
| - | [[Category: | + | [[Category: Garcia-Pino A]] |
| - | [[Category: Moonens | + | [[Category: Moonens K]] |
| - | [[Category: | + | [[Category: Van Molle I]] |
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Current revision
FaeE-FaeG chaperone-major pilin complex of F4 ad fimbriae
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