2col: Difference between revisions

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[[Image:2col.gif|left|200px]]<br /><applet load="2col" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:2col.gif|left|200px]]
caption="2col, resolution 2.2&Aring;" />
 
'''Crystal structure analysis of CyaA/C-Cam with Pyrophosphate'''<br />
{{Structure
|PDB= 2col |SIZE=350|CAPTION= <scene name='initialview01'>2col</scene>, resolution 2.2&Aring;
|SITE=
|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> and <scene name='pdbligand=POP:PYROPHOSPHATE 2-'>POP</scene>
|ACTIVITY= [http://en.wikipedia.org/wiki/Adenylate_cyclase Adenylate cyclase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.6.1.1 4.6.1.1]
|GENE=
}}
 
'''Crystal structure analysis of CyaA/C-Cam with Pyrophosphate'''
 


==Overview==
==Overview==
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==About this Structure==
==About this Structure==
2COL is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Bordetella_pertussis Bordetella pertussis] and [http://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis] with <scene name='pdbligand=CA:'>CA</scene>, <scene name='pdbligand=MG:'>MG</scene> and <scene name='pdbligand=POP:'>POP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Adenylate_cyclase Adenylate cyclase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.6.1.1 4.6.1.1] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2COL OCA].  
2COL is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Bordetella_pertussis Bordetella pertussis] and [http://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2COL OCA].  


==Reference==
==Reference==
Structural basis for the interaction of Bordetella pertussis adenylyl cyclase toxin with calmodulin., Guo Q, Shen Y, Lee YS, Gibbs CS, Mrksich M, Tang WJ, EMBO J. 2005 Sep 21;24(18):3190-201. Epub 2005 Sep 1. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16138079 16138079]
Structural basis for the interaction of Bordetella pertussis adenylyl cyclase toxin with calmodulin., Guo Q, Shen Y, Lee YS, Gibbs CS, Mrksich M, Tang WJ, EMBO J. 2005 Sep 21;24(18):3190-201. Epub 2005 Sep 1. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16138079 16138079]
[[Category: Adenylate cyclase]]
[[Category: Adenylate cyclase]]
[[Category: Bordetella pertussis]]
[[Category: Bordetella pertussis]]
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[[Category: lyase]]
[[Category: lyase]]


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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:18:03 2008''

Revision as of 17:18, 20 March 2008

File:2col.gif


PDB ID 2col

Drag the structure with the mouse to rotate
, resolution 2.2Å
Ligands: , and
Activity: Adenylate cyclase, with EC number 4.6.1.1
Coordinates: save as pdb, mmCIF, xml



Crystal structure analysis of CyaA/C-Cam with Pyrophosphate


OverviewOverview

CyaA is crucial for colonization by Bordetella pertussis, the etiologic agent of whooping cough. Here we report crystal structures of the adenylyl cyclase domain (ACD) of CyaA with the C-terminal domain of calmodulin. Four discrete regions of CyaA bind calcium-loaded calmodulin with a large buried contact surface. Of those, a tryptophan residue (W242) at an alpha-helix of CyaA makes extensive contacts with the calcium-induced, hydrophobic pocket of calmodulin. Mutagenic analyses show that all four regions of CyaA contribute to calmodulin binding and the calmodulin-induced conformational change of CyaA is crucial for catalytic activation. A crystal structure of CyaA-calmodulin with adefovir diphosphate, the metabolite of an approved antiviral drug, reveals the location of catalytic site of CyaA and how adefovir diphosphate tightly binds CyaA. The ACD of CyaA shares a similar structure and mechanism of activation with anthrax edema factor (EF). However, the interactions of CyaA with calmodulin completely diverge from those of EF. This provides molecular details of how two structurally homologous bacterial toxins evolved divergently to bind calmodulin, an evolutionarily conserved calcium sensor.

About this StructureAbout this Structure

2COL is a Protein complex structure of sequences from Bordetella pertussis and Xenopus laevis. Full crystallographic information is available from OCA.

ReferenceReference

Structural basis for the interaction of Bordetella pertussis adenylyl cyclase toxin with calmodulin., Guo Q, Shen Y, Lee YS, Gibbs CS, Mrksich M, Tang WJ, EMBO J. 2005 Sep 21;24(18):3190-201. Epub 2005 Sep 1. PMID:16138079

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