1zot: Difference between revisions

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[[Image:1zot.gif|left|200px]]<br /><applet load="1zot" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:1zot.gif|left|200px]]
caption="1zot, resolution 2.20&Aring;" />
 
'''crystal structure analysis of the CyaA/C-Cam with PMEAPP'''<br />
{{Structure
|PDB= 1zot |SIZE=350|CAPTION= <scene name='initialview01'>1zot</scene>, resolution 2.20&Aring;
|SITE=
|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> and <scene name='pdbligand=EMA:(ADENIN-9-YL-ETHOXYMETHYL)-HYDROXYPHOSPHINYL-DIPHOSPHATE'>EMA</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 the CyaA/C-Cam with PMEAPP'''
 


==Overview==
==Overview==
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==About this Structure==
==About this Structure==
1ZOT 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/Homo_sapiens Homo sapiens] with <scene name='pdbligand=CA:'>CA</scene>, <scene name='pdbligand=MG:'>MG</scene> and <scene name='pdbligand=EMA:'>EMA</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=1ZOT OCA].  
1ZOT is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Bordetella_pertussis Bordetella pertussis] and [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZOT 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: pmeapp]]
[[Category: pmeapp]]


''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:17:39 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:38:05 2008''

Revision as of 16:38, 20 March 2008

File:1zot.gif


PDB ID 1zot

Drag the structure with the mouse to rotate
, resolution 2.20Å
Ligands: , and
Activity: Adenylate cyclase, with EC number 4.6.1.1
Coordinates: save as pdb, mmCIF, xml



crystal structure analysis of the CyaA/C-Cam with PMEAPP


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.

DiseaseDisease

Known diseases associated with this structure: Cavernous malformations of CNS and retina OMIM:[604214], Cerebral cavernous malformations-1 OMIM:[604214], Hyperkeratotic cutaneous capillary-venous malformations associated with cerebral capillary malformations OMIM:[604214], Leukemia, acute T-cell lymphoblastic OMIM:[603025], Leukemia, acute myeloid OMIM:[603025]

About this StructureAbout this Structure

1ZOT is a Protein complex structure of sequences from Bordetella pertussis and Homo sapiens. 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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