1acc
From Proteopedia
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| - | [[Image:1acc.gif|left|200px]] | + | [[Image:1acc.gif|left|200px]] |
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| - | '''ANTHRAX PROTECTIVE ANTIGEN''' | + | {{Structure |
| + | |PDB= 1acc |SIZE=350|CAPTION= <scene name='initialview01'>1acc</scene>, resolution 2.1Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=CA:CALCIUM ION'>CA</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''ANTHRAX PROTECTIVE ANTIGEN''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1ACC is a [ | + | 1ACC is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_anthracis Bacillus anthracis]. The following page contains interesting information on the relation of 1ACC with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb28_1.html Anthrax Toxin]]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ACC OCA]. |
==Reference== | ==Reference== | ||
| - | Crystal structure of the anthrax toxin protective antigen., Petosa C, Collier RJ, Klimpel KR, Leppla SH, Liddington RC, Nature. 1997 Feb 27;385(6619):833-8. PMID:[http:// | + | Crystal structure of the anthrax toxin protective antigen., Petosa C, Collier RJ, Klimpel KR, Leppla SH, Liddington RC, Nature. 1997 Feb 27;385(6619):833-8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9039918 9039918] |
[[Category: Anthrax Toxin]] | [[Category: Anthrax Toxin]] | ||
[[Category: Bacillus anthracis]] | [[Category: Bacillus anthracis]] | ||
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[[Category: toxin]] | [[Category: toxin]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 09:55:41 2008'' |
Revision as of 07:55, 20 March 2008
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| , resolution 2.1Å | |||||||
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
ANTHRAX PROTECTIVE ANTIGEN
Overview
Protective antigen (PA) is the central component of the three-part protein toxin secreted by Bacillus anthracis, the organism responsible for anthrax. After proteolytic activation on the host cell surface, PA forms a membrane-inserting heptamer that translocates the toxic enzymes, oedema factor and lethal factor, into the cytosol. PA, which has a relative molecular mass of 83,000 (M(r) 83K), can also translocate heterologous proteins, and is being evaluated for use as a general protein delivery system. Here we report the crystal structure of monomeric PA at 2.1 A resolution and the water-soluble heptamer at 4.5 A resolution. The monomer is organized mainly into antiparallel beta-sheets and has four domains: an amino-terminal domain (domain 1) containing two calcium ions and the cleavage site for activating proteases; a heptamerization domain (domain 2) containing a large flexible loop implicated in membrane insertion; a small domain of unknown function (domain 3); and a carboxy-terminal receptor-binding domain (domain 4). Removal of a 20K amino-terminal fragment from domain 1 allows the assembly of the heptamer, a ring-shaped structure with a negatively charged lumen, and exposes a large hydrophobic surface for binding the toxic enzymes. We propose a model of pH-dependent membrane insertion involving the formation of a porin-like, membrane-spanning beta-barrel.
About this Structure
1ACC is a Single protein structure of sequence from Bacillus anthracis. The following page contains interesting information on the relation of 1ACC with [Anthrax Toxin]. Full crystallographic information is available from OCA.
Reference
Crystal structure of the anthrax toxin protective antigen., Petosa C, Collier RJ, Klimpel KR, Leppla SH, Liddington RC, Nature. 1997 Feb 27;385(6619):833-8. PMID:9039918
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