1cjk: Difference between revisions

Revision as of 20:50, 30 June 2008

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File:1cjk.png

Template:STRUCTURE 1cjk

COMPLEX OF GS-ALPHA WITH THE CATALYTIC DOMAINS OF MAMMALIAN ADENYLYL CYCLASE: COMPLEX WITH ADENOSINE 5'-(ALPHA THIO)-TRIPHOSPHATE (RP), MG, AND MNCOMPLEX OF GS-ALPHA WITH THE CATALYTIC DOMAINS OF MAMMALIAN ADENYLYL CYCLASE: COMPLEX WITH ADENOSINE 5'-(ALPHA THIO)-TRIPHOSPHATE (RP), MG, AND MN

Template:ABSTRACT PUBMED 10427002

About this StructureAbout this Structure

1CJK is a Protein complex structure of sequences from Bos taurus, Canis lupus familiaris and Rattus norvegicus. Full crystallographic information is available from OCA.

ReferenceReference

Two-metal-Ion catalysis in adenylyl cyclase., Tesmer JJ, Sunahara RK, Johnson RA, Gosselin G, Gilman AG, Sprang SR, Science. 1999 Jul 30;285(5428):756-60. PMID:10427002

Page seeded by OCA on Mon Jun 30 20:50:13 2008

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OCA

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-[[Image:1cjk.gif|left|200px]]
+{{Seed}}
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 {{STRUCTURE_1cjk|  PDB=1cjk  |  SCENE=  }}
-'''COMPLEX OF GS-ALPHA WITH THE CATALYTIC DOMAINS OF MAMMALIAN ADENYLYL CYCLASE: COMPLEX WITH ADENOSINE 5'-(ALPHA THIO)-TRIPHOSPHATE (RP), MG, AND MN'''
+===COMPLEX OF GS-ALPHA WITH THE CATALYTIC DOMAINS OF MAMMALIAN ADENYLYL CYCLASE: COMPLEX WITH ADENOSINE 5'-(ALPHA THIO)-TRIPHOSPHATE (RP), MG, AND MN===
-==Overview==
+<!--
-Adenylyl cyclase (AC) converts adenosine triphosphate (ATP) to cyclic adenosine monophosphate, a ubiquitous second messenger that regulates many cellular functions. Recent structural studies have revealed much about the structure and function of mammalian AC but have not fully defined its active site or catalytic mechanism. Four crystal structures were determined of the catalytic domains of AC in complex with two different ATP analogs and various divalent metal ions. These structures provide a model for the enzyme-substrate complex and conclusively demonstrate that two metal ions bind in the active site. The similarity of the active site of AC to those of DNA polymerases suggests that the enzymes catalyze phosphoryl transfer by the same two-metal-ion mechanism and likely have evolved from a common ancestor.
+The line below this paragraph, {{ABSTRACT_PUBMED_10427002}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 10427002 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_10427002}}
 ==About this Structure==
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 [[Category: Hydrolase]]
 [[Category: Signal transducing protein]]
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