3etz: Difference between revisions
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<StructureSection load='3etz' size='340' side='right'caption='[[3etz]], [[Resolution|resolution]] 2.00Å' scene=''> | <StructureSection load='3etz' size='340' side='right'caption='[[3etz]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3etz]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[3etz]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Fusobacterium_nucleatum Fusobacterium nucleatum]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2gld 2gld]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ETZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ETZ FirstGlance]. <br> | ||
</td></tr><tr id=' | </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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3etz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3etz OCA], [https://pdbe.org/3etz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3etz RCSB], [https://www.ebi.ac.uk/pdbsum/3etz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3etz ProSAT]</span></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=3etz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3etz OCA], [https://pdbe.org/3etz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3etz RCSB], [https://www.ebi.ac.uk/pdbsum/3etz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3etz ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/Q5I6B0_FUSNU Q5I6B0_FUSNU] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Fusobacterium nucleatum]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Han | [[Category: Han YW]] | ||
[[Category: Nithianantham | [[Category: Nithianantham S]] | ||
[[Category: Shoham | [[Category: Shoham M]] | ||
[[Category: Wu | [[Category: Wu N]] | ||
[[Category: Xu | [[Category: Xu M]] | ||
Latest revision as of 16:13, 26 July 2023
Crystal structure of bacterial adhesin FadA L76A mutantCrystal structure of bacterial adhesin FadA L76A mutant
Structural highlights
FunctionPublication Abstract from PubMedMany bacterial appendages have filamentous structures, often composed of repeating monomers assembled in a head-to-tail manner. The mechanisms of such linkages vary. We report here a novel protein oligomerization motif identified in the FadA adhesin from the Gram-negative bacterium Fusobacterium nucleatum. The 2.0 A crystal structure of the secreted form of FadA (mFadA) reveals two antiparallel -helices connected by an intervening eight-residue hairpin loop. Leucine-leucine contacts play a prominent dual intra- and inter-molecular role in the structure and function of FadA. First, they comprise the main association between the two helical arms of the monomer; second, they mediate the head-to-tail association of monomers to form the elongated polymers. This leucine-mediated filamentous assembly of FadA molecules constitutes a novel structural motif termed the "leucine chain". The essential role of these residues in FadA is corroborated by mutagenesis of selected leucine residues, which leads to the abrogation of oligomerization, filament formation, and binding to host cells. Crystal structure of FadA adhesin from fusobacterium nucleatum reveals a novel oligomerization motif: The leucine chain.,Nithianantham S, Xu M, Yamada M, Ikegami A, Shoham M, Han YW J Biol Chem. 2008 Nov 7. PMID:18996848[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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