1cjk: Difference between revisions

Line 1:

[[Image:1cjk.~~gif~~|left|200px]]

[[Image:1cjk.png|left|200px]]

<!--

Line 9:

Line 10:

~~'''~~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.

-->

==About this Structure==

Line 31:

Line 35:

[[Category: Hydrolase]]

[[Category: Signal transducing protein]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Fri May 2 12~~:48:14 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 20:50:13 2008''

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools

@@ Line 1: / Line 1: @@
-[[Image:1cjk.gif|left|200px]]
+{{Seed}}
+[[Image:1cjk.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{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==
@@ Line 31: / Line 35: @@
 [[Category: Hydrolase]]
 [[Category: Signal transducing protein]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 12:48:14 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 20:50:13 2008''