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| | ==Crystal Structure of Anthrax Protective Antigen (Membrane Insertion Loop Deleted) Mutant S337C N664C to 2.06-A resolution== | | ==Crystal Structure of Anthrax Protective Antigen (Membrane Insertion Loop Deleted) Mutant S337C N664C to 2.06-A resolution== |
| - | <StructureSection load='3tey' size='340' side='right' caption='[[3tey]], [[Resolution|resolution]] 2.12Å' scene=''> | + | <StructureSection load='3tey' size='340' side='right'caption='[[3tey]], [[Resolution|resolution]] 2.12Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3tey]] is a 1 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=3TEY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3TEY FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3tey]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_anthracis Bacillus anthracis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TEY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3TEY 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> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.12Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3tew|3tew]], [[3tex|3tex]], [[3tez|3tez]]</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BXA0164, GBAA_pXO1_0164, pag, pagA, PX01, pXO1-110 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1392 Bacillus anthracis])</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=3tey FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tey OCA], [https://pdbe.org/3tey PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3tey RCSB], [https://www.ebi.ac.uk/pdbsum/3tey PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3tey ProSAT]</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=3tey FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tey OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3tey RCSB], [http://www.ebi.ac.uk/pdbsum/3tey PDBsum]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/PAG_BACAN PAG_BACAN] One of the three proteins composing the anthrax toxin, the agent which infects many mammalian species and that may cause death. PA binds to a receptor (ATR) in sensitive eukaryotic cells, thereby facilitating the translocation of the enzymatic toxin components, edema factor and lethal factor, across the target cell membrane. PA associated with LF causes death when injected, PA associated with EF produces edema. PA induces immunity to infection with anthrax. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| | </div> | | </div> |
| - | | + | <div class="pdbe-citations 3tey" style="background-color:#fffaf0;"></div> |
| - | ==See Also== | + | |
| - | *[[Anthrax protective antigen|Anthrax protective antigen]]
| + | |
| | == References == | | == References == |
| | <references/> | | <references/> |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Bacillus anthracis]] | | [[Category: Bacillus anthracis]] |
| - | [[Category: Feld, G K]] | + | [[Category: Large Structures]] |
| - | [[Category: Krantz, B A]] | + | [[Category: Feld GK]] |
| - | [[Category: Protein transport]] | + | [[Category: Krantz BA]] |
| - | [[Category: Toxin]]
| + | |
| Structural highlights
Function
PAG_BACAN One of the three proteins composing the anthrax toxin, the agent which infects many mammalian species and that may cause death. PA binds to a receptor (ATR) in sensitive eukaryotic cells, thereby facilitating the translocation of the enzymatic toxin components, edema factor and lethal factor, across the target cell membrane. PA associated with LF causes death when injected, PA associated with EF produces edema. PA induces immunity to infection with anthrax.
Publication Abstract from PubMed
The three protein components of anthrax toxin are nontoxic individually, but they form active holotoxin complexes upon assembly. The role of the protective antigen (PA) component of the toxin is to deliver two other enzyme components, lethal factor and edema factor, across the plasma membrane and into the cytoplasm of target cells. PA is produced as a proprotein, which must be proteolytically activated; generally, cell surface activation is mediated by a furin family protease. Activated PA can then assemble into one of two noninterconverting oligomers, a homoheptamer and a homooctamer, which have unique properties. Herein we describe molecular determinants that influence the stoichiometry of PA in toxin complexes. By tethering PA domain 4 (D4) to domain 2 with two different-length cross-links, we can control the relative proportions of PA heptamers and octamers. The longer cross-link favors octamer formation, whereas the shorter one favors formation of the heptamer. X-ray crystal structures of PA (up to 1.45 A resolution), including these cross-linked PA constructs, reveal that a hinge-like movement of D4 correlates with the relative preference for each oligomeric architecture. Furthermore, we report the conformation of the flexible loop containing the furin cleavage site and show that, for efficient processing, the furin site cannot be moved ~5 or 6 residues within the loop. We propose that there are different orientations of D4 relative to the main body of PA that favor the formation of either the heptamer or the octamer.
Domain flexibility modulates the heterogeneous assembly mechanism of anthrax toxin protective antigen.,Feld GK, Kintzer AF, Tang II, Thoren KL, Krantz BA J Mol Biol. 2012 Jan 6;415(1):159-74. Epub 2011 Oct 31. PMID:22063095[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Feld GK, Kintzer AF, Tang II, Thoren KL, Krantz BA. Domain flexibility modulates the heterogeneous assembly mechanism of anthrax toxin protective antigen. J Mol Biol. 2012 Jan 6;415(1):159-74. Epub 2011 Oct 31. PMID:22063095 doi:10.1016/j.jmb.2011.10.035
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