1wc3: Difference between revisions

Revision as of 16:42, 21 February 2008

SOLUBLE ADENYLYL CYCLASE CYAC FROM S. PLATENSIS IN COMPLEX WITH ALPHA,BETA-METHYLENE-ATP AND STRONTIUM

OverviewOverview

In an evolutionarily conserved signaling pathway, 'soluble' adenylyl cyclases (sACs) synthesize the ubiquitous second messenger cyclic adenosine 3',5'-monophosphate (cAMP) in response to bicarbonate and calcium signals. Here, we present crystal structures of a cyanobacterial sAC enzyme in complex with ATP analogs, calcium and bicarbonate, which represent distinct catalytic states of the enzyme. The structures reveal that calcium occupies the first ion-binding site and directly mediates nucleotide binding. The single ion-occupied, nucleotide-bound state defines a novel, open adenylyl cyclase state. In contrast, bicarbonate increases the catalytic rate by inducing marked active site closure and recruiting a second, catalytic ion. The phosphates of the bound substrate analogs are rearranged, which would facilitate product formation and release. The mechanisms of calcium and bicarbonate sensing define a reaction pathway involving active site closure and metal recruitment that may be universal for class III cyclases.

About this StructureAbout this Structure

1WC3 is a Single protein structure of sequence from Arthrospira platensis with and as ligands. Active as Adenylate cyclase, with EC number 4.6.1.1 Full crystallographic information is available from OCA.

ReferenceReference

Bicarbonate activation of adenylyl cyclase via promotion of catalytic active site closure and metal recruitment., Steegborn C, Litvin TN, Levin LR, Buck J, Wu H, Nat Struct Mol Biol. 2005 Jan;12(1):32-7. Epub 2004 Dec 26. PMID:15619637

Page seeded by OCA on Thu Feb 21 15:42:41 2008

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OCA

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-[[Image:1wc3.gif|left|200px]]<br /><applet load="1wc3" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1wc3.gif|left|200px]]<br /><applet load="1wc3" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1wc3, resolution 1.9&Aring;" />
 '''SOLUBLE ADENYLYL CYCLASE CYAC FROM S. PLATENSIS IN COMPLEX WITH ALPHA,BETA-METHYLENE-ATP AND STRONTIUM'''<br />
 ==Overview==
-In an evolutionarily conserved signaling pathway, 'soluble' adenylyl, cyclases (sACs) synthesize the ubiquitous second messenger cyclic, adenosine 3',5'-monophosphate (cAMP) in response to bicarbonate and, calcium signals. Here, we present crystal structures of a cyanobacterial, sAC enzyme in complex with ATP analogs, calcium and bicarbonate, which, represent distinct catalytic states of the enzyme. The structures reveal, that calcium occupies the first ion-binding site and directly mediates, nucleotide binding. The single ion-occupied, nucleotide-bound state, defines a novel, open adenylyl cyclase state. In contrast, bicarbonate, increases the catalytic rate by inducing marked active site closure and, recruiting a second, catalytic ion. The phosphates of the bound substrate, analogs are rearranged, which would facilitate product formation and, release. The mechanisms of calcium and bicarbonate sensing define a, reaction pathway involving active site closure and metal recruitment that, may be universal for class III cyclases.
+In an evolutionarily conserved signaling pathway, 'soluble' adenylyl cyclases (sACs) synthesize the ubiquitous second messenger cyclic adenosine 3',5'-monophosphate (cAMP) in response to bicarbonate and calcium signals. Here, we present crystal structures of a cyanobacterial sAC enzyme in complex with ATP analogs, calcium and bicarbonate, which represent distinct catalytic states of the enzyme. The structures reveal that calcium occupies the first ion-binding site and directly mediates nucleotide binding. The single ion-occupied, nucleotide-bound state defines a novel, open adenylyl cyclase state. In contrast, bicarbonate increases the catalytic rate by inducing marked active site closure and recruiting a second, catalytic ion. The phosphates of the bound substrate analogs are rearranged, which would facilitate product formation and release. The mechanisms of calcium and bicarbonate sensing define a reaction pathway involving active site closure and metal recruitment that may be universal for class III cyclases.
 ==About this Structure==
-WC3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Arthrospira_platensis Arthrospira platensis] with SR and APC 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=1WC3 OCA].
+WC3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Arthrospira_platensis Arthrospira platensis] with <scene name='pdbligand=SR:'>SR</scene> and <scene name='pdbligand=APC:'>APC</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=1WC3 OCA].
 ==Reference==
@@ Line 15: / Line 15: @@
 [[Category: Single protein]]
 [[Category: Buck, J.]]
-[[Category: Levin, L.R.]]
+[[Category: Levin, L R.]]
-[[Category: Litvin, T.N.]]
+[[Category: Litvin, T N.]]
 [[Category: Steegborn, C.]]
 [[Category: Wu, H.]]
@@ Line 26: / Line 26: @@
 [[Category: soluble adenylyl cyclase]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sat Nov 24 23:42:29 2007''
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