3etx: Difference between revisions
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==Crystal structure of bacterial adhesin FadA L14A mutant== | ==Crystal structure of bacterial adhesin FadA L14A mutant== | ||
<StructureSection load='3etx' size='340' side='right' caption='[[3etx]], [[Resolution|resolution]] 3.00Å' scene=''> | <StructureSection load='3etx' size='340' side='right'caption='[[3etx]], [[Resolution|resolution]] 3.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3etx]] is a 3 chain structure with sequence from [ | <table><tr><td colspan='2'>[[3etx]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_fusiformis"_veillon_and_zuber_1898 "bacillus fusiformis" veillon and zuber 1898]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2bc6 2bc6]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ETX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ETX FirstGlance]. <br> | ||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3etw|3etw]], [[3ety|3ety]], [[3etz|3etz]]</td></tr> | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3etw|3etw]], [[3ety|3ety]], [[3etz|3etz]]</div></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">fadA ([ | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">fadA ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=851 "Bacillus fusiformis" Veillon and Zuber 1898])</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3etx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3etx OCA], [https://pdbe.org/3etx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3etx RCSB], [https://www.ebi.ac.uk/pdbsum/3etx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3etx ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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</div> | </div> | ||
<div class="pdbe-citations 3etx" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 3etx" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Adhesin 3D structures|Adhesin 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Bacillus fusiformis veillon and zuber 1898]] | [[Category: Bacillus fusiformis veillon and zuber 1898]] | ||
[[Category: Large Structures]] | |||
[[Category: Han, Y W]] | [[Category: Han, Y W]] | ||
[[Category: Nithianantham, S]] | [[Category: Nithianantham, S]] | ||
Revision as of 22:46, 20 October 2021
Crystal structure of bacterial adhesin FadA L14A mutantCrystal structure of bacterial adhesin FadA L14A mutant
Structural highlights
Publication 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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