1zot: Difference between revisions

Revision as of 22:08, 27 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1zot.png

Template:STRUCTURE 1zot

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

Template:ABSTRACT PUBMED 16138079

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

Page seeded by OCA on Sun Jul 27 22:07:51 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:1zot.gif|left|200px]]
+{{Seed}}
+[[Image:1zot.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1zot|  PDB=1zot  |  SCENE=  }}
-'''crystal structure analysis of the CyaA/C-Cam with PMEAPP'''
+===crystal structure analysis of the CyaA/C-Cam with PMEAPP===
-==Overview==
+<!--
-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_16138079}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 16138079 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_16138079}}
 ==About this Structure==
@@ Line 31: / Line 35: @@
 [[Category: Cyaa]]
 [[Category: Pmeapp]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 17:53:26 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 22:07:51 2008''