1tzn: Difference between revisions

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New page: left|200px<br /> <applet load="1tzn" size="450" color="white" frame="true" align="right" spinBox="true" caption="1tzn, resolution 4.30Å" /> '''Crystal Structure o...
 
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[[Image:1tzn.gif|left|200px]]<br />
[[Image:1tzn.gif|left|200px]]<br /><applet load="1tzn" size="350" color="white" frame="true" align="right" spinBox="true"  
<applet load="1tzn" size="450" color="white" frame="true" align="right" spinBox="true"  
caption="1tzn, resolution 4.30&Aring;" />
caption="1tzn, resolution 4.30&Aring;" />
'''Crystal Structure of the Anthrax Toxin Protective Antigen Heptameric Prepore bound to the VWA domain of CMG2, an anthrax toxin receptor'''<br />
'''Crystal Structure of the Anthrax Toxin Protective Antigen Heptameric Prepore bound to the VWA domain of CMG2, an anthrax toxin receptor'''<br />


==Overview==
==Overview==
After binding to cellular receptors and proteolytic activation, the, protective antigen component of anthrax toxin forms a heptameric prepore., The prepore later undergoes pH-dependent conversion to a pore, mediating, translocation of the edema and lethal factors to the cytosol. We describe, structures of the prepore (3.6 A) and a prepore:receptor complex (4.3 A), that reveal the location of pore-forming loops and an unexpected, interaction of the receptor with the pore-forming domain. Lower pH is, required for prepore-to-pore conversion in the presence of the receptor, indicating that this interaction regulates pH-dependent pore formation. We, present an example of a receptor negatively regulating pH-dependent, membrane insertion.
After binding to cellular receptors and proteolytic activation, the protective antigen component of anthrax toxin forms a heptameric prepore. The prepore later undergoes pH-dependent conversion to a pore, mediating translocation of the edema and lethal factors to the cytosol. We describe structures of the prepore (3.6 A) and a prepore:receptor complex (4.3 A) that reveal the location of pore-forming loops and an unexpected interaction of the receptor with the pore-forming domain. Lower pH is required for prepore-to-pore conversion in the presence of the receptor, indicating that this interaction regulates pH-dependent pore formation. We present an example of a receptor negatively regulating pH-dependent membrane insertion.


==Disease==
==Disease==
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==About this Structure==
==About this Structure==
1TZN is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Bacillus_anthracis Bacillus anthracis] and [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with CA and MG as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1TZN OCA].  
1TZN is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Bacillus_anthracis Bacillus anthracis] and [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=CA:'>CA</scene> and <scene name='pdbligand=MG:'>MG</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TZN OCA].  


==Reference==
==Reference==
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Collier, R.J.]]
[[Category: Collier, R J.]]
[[Category: Lacy, D.B.]]
[[Category: Lacy, D B.]]
[[Category: Melnyk, R.A.]]
[[Category: Melnyk, R A.]]
[[Category: Wigelsworth, D.J.]]
[[Category: Wigelsworth, D J.]]
[[Category: CA]]
[[Category: CA]]
[[Category: MG]]
[[Category: MG]]
[[Category: heptamer]]
[[Category: heptamer]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 19:29:56 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:19:03 2008''

Revision as of 16:19, 21 February 2008

File:1tzn.gif


1tzn, resolution 4.30Å

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Crystal Structure of the Anthrax Toxin Protective Antigen Heptameric Prepore bound to the VWA domain of CMG2, an anthrax toxin receptor

OverviewOverview

After binding to cellular receptors and proteolytic activation, the protective antigen component of anthrax toxin forms a heptameric prepore. The prepore later undergoes pH-dependent conversion to a pore, mediating translocation of the edema and lethal factors to the cytosol. We describe structures of the prepore (3.6 A) and a prepore:receptor complex (4.3 A) that reveal the location of pore-forming loops and an unexpected interaction of the receptor with the pore-forming domain. Lower pH is required for prepore-to-pore conversion in the presence of the receptor, indicating that this interaction regulates pH-dependent pore formation. We present an example of a receptor negatively regulating pH-dependent membrane insertion.

DiseaseDisease

Known diseases associated with this structure: Fibromatosis, juvenile hyaline OMIM:[608041], Hyalinosis, infantile systemic OMIM:[608041]

About this StructureAbout this Structure

1TZN is a Protein complex structure of sequences from Bacillus anthracis and Homo sapiens with and as ligands. Full crystallographic information is available from OCA.

ReferenceReference

Structure of heptameric protective antigen bound to an anthrax toxin receptor: a role for receptor in pH-dependent pore formation., Lacy DB, Wigelsworth DJ, Melnyk RA, Harrison SC, Collier RJ, Proc Natl Acad Sci U S A. 2004 Sep 7;101(36):13147-51. Epub 2004 Aug 23. PMID:15326297

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