1cju: Difference between revisions

Revision as of 13:06, 21 February 2008

COMPLEX OF GS-ALPHA WITH THE CATALYTIC DOMAINS OF MAMMALIAN ADENYLYL CYCLASE: COMPLEX WITH BETA-L-2',3'-DIDEOXYATP AND MG

OverviewOverview

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.

About this StructureAbout this Structure

1CJU is a Protein complex structure of sequences from Bos taurus, Canis lupus familiaris and Rattus norvegicus with , , , and as ligands. Active as Adenylate cyclase, with EC number 4.6.1.1 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 Thu Feb 21 12:06:49 2008

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

OCA

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-[[Image:1cju.gif|left|200px]]<br /><applet load="1cju" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1cju.gif|left|200px]]<br /><applet load="1cju" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1cju, resolution 2.80&Aring;" />
 '''COMPLEX OF GS-ALPHA WITH THE CATALYTIC DOMAINS OF MAMMALIAN ADENYLYL CYCLASE: COMPLEX WITH BETA-L-2',3'-DIDEOXYATP AND MG'''<br />
 ==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.
+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.
 ==About this Structure==
-CJU is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus], [http://en.wikipedia.org/wiki/Canis_lupus_familiaris Canis lupus familiaris] and [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with MG, CL, GSP, FOK and DAD 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1CJU OCA].
+CJU is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus], [http://en.wikipedia.org/wiki/Canis_lupus_familiaris Canis lupus familiaris] and [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=CL:'>CL</scene>, <scene name='pdbligand=GSP:'>GSP</scene>, <scene name='pdbligand=FOK:'>FOK</scene> and <scene name='pdbligand=DAD:'>DAD</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=1CJU OCA].
 ==Reference==
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 [[Category: Protein complex]]
 [[Category: Rattus norvegicus]]
-[[Category: Sprang, S.R.]]
+[[Category: Sprang, S R.]]
-[[Category: Tesmer, J.J.G.]]
+[[Category: Tesmer, J J.G.]]
 [[Category: CL]]
 [[Category: DAD]]
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 [[Category: signal transducing protein]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 12:31:19 2007''
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