3kwv
From Proteopedia
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- | [[ | + | ==Structural basis for the unfolding of anthrax lethal factor by protective antigen oligomers== |
+ | <StructureSection load='3kwv' size='340' side='right' caption='[[3kwv]], [[Resolution|resolution]] 3.10Å' scene=''> | ||
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[3kwv]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacillus_anthracis Bacillus anthracis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3KWV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3KWV FirstGlance]. <br> | ||
+ | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr> | ||
+ | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">pagA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1392 Bacillus anthracis]), lef ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1392 Bacillus anthracis])</td></tr> | ||
+ | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Anthrax_lethal_factor_endopeptidase Anthrax lethal factor endopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.83 3.4.24.83] </span></td></tr> | ||
+ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3kwv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3kwv OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3kwv RCSB], [http://www.ebi.ac.uk/pdbsum/3kwv PDBsum]</span></td></tr> | ||
+ | </table> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | The protein transporter anthrax lethal toxin is composed of protective antigen (PA), a transmembrane translocase, and lethal factor (LF), a cytotoxic enzyme. After its assembly into holotoxin complexes, PA forms an oligomeric channel that unfolds LF and translocates it into the host cell. We report the crystal structure of the core of a lethal toxin complex to 3.1-A resolution; the structure contains a PA octamer bound to four LF PA-binding domains (LF(N)). The first alpha-helix and beta-strand of each LF(N) unfold and dock into a deep amphipathic cleft on the surface of the PA octamer, which we call the alpha clamp. The alpha clamp possesses nonspecific polypeptide binding activity and is functionally relevant to efficient holotoxin assembly, PA octamer formation, and LF unfolding and translocation. This structure provides insight into the mechanism of translocation-coupled protein unfolding. | ||
- | + | Structural basis for the unfolding of anthrax lethal factor by protective antigen oligomers.,Feld GK, Thoren KL, Kintzer AF, Sterling HJ, Tang II, Greenberg SG, Williams ER, Krantz BA Nat Struct Mol Biol. 2010 Oct 31. PMID:21037566<ref>PMID:21037566</ref> | |
- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | + | </div> | |
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==See Also== | ==See Also== | ||
*[[Anthrax Lethal Factor|Anthrax Lethal Factor]] | *[[Anthrax Lethal Factor|Anthrax Lethal Factor]] | ||
*[[Anthrax protective antigen|Anthrax protective antigen]] | *[[Anthrax protective antigen|Anthrax protective antigen]] | ||
- | + | == References == | |
- | == | + | <references/> |
- | < | + | __TOC__ |
+ | </StructureSection> | ||
[[Category: Anthrax lethal factor endopeptidase]] | [[Category: Anthrax lethal factor endopeptidase]] | ||
[[Category: Bacillus anthracis]] | [[Category: Bacillus anthracis]] | ||
- | [[Category: Feld, G K | + | [[Category: Feld, G K]] |
- | [[Category: Kintzer, A F | + | [[Category: Kintzer, A F]] |
- | [[Category: Krantz, B A | + | [[Category: Krantz, B A]] |
- | + | ||
[[Category: Cleavage on pair of basic residue]] | [[Category: Cleavage on pair of basic residue]] | ||
[[Category: Hydrolase]] | [[Category: Hydrolase]] |
Revision as of 08:51, 9 December 2014
Structural basis for the unfolding of anthrax lethal factor by protective antigen oligomers
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Categories: Anthrax lethal factor endopeptidase | Bacillus anthracis | Feld, G K | Kintzer, A F | Krantz, B A | Cleavage on pair of basic residue | Hydrolase | Lethal factor | Lethal toxin | Metal-binding | Metalloprotease | Octamer | Protease | Protective antigen | Protein translocation | Protein transport | Protein unfolding | Secreted | Toxin | Toxin-protein transport complex | Virulence