1wc6

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[[Image:1wc6.gif|left|200px]]<br /><applet load="1wc6" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1wc6.gif|left|200px]]
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caption="1wc6, resolution 2.51&Aring;" />
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'''SOLUBLE ADENYLYL CYCLASE CYAC FROM S. PLATENSIS IN COMPLEX WITH RP-ATPALPHAS IN PRESENCE OF BICARBONATE'''<br />
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{{Structure
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|PDB= 1wc6 |SIZE=350|CAPTION= <scene name='initialview01'>1wc6</scene>, resolution 2.51&Aring;
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|SITE= <scene name='pdbsite=AC1:Mg+Binding+Site+For+Chain+C'>AC1</scene>
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|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> and <scene name='pdbligand=TAT:ADENOSINE-5'-RP-ALPHA-THIO-TRIPHOSPHATE'>TAT</scene>
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|ACTIVITY= [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]
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|GENE=
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}}
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'''SOLUBLE ADENYLYL CYCLASE CYAC FROM S. PLATENSIS IN COMPLEX WITH RP-ATPALPHAS IN PRESENCE OF BICARBONATE'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1WC6 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=MG:'>MG</scene> and <scene name='pdbligand=TAT:'>TAT</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] Known structural/functional Site: <scene name='pdbsite=AC1:Mg+Binding+Site+For+Chain+C'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WC6 OCA].
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1WC6 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Arthrospira_platensis Arthrospira platensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WC6 OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15619637 15619637]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/15619637 15619637]
[[Category: Adenylate cyclase]]
[[Category: Adenylate cyclase]]
[[Category: Arthrospira platensis]]
[[Category: Arthrospira platensis]]
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[[Category: soluble adenylyl cyclase]]
[[Category: soluble adenylyl cyclase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:42:44 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:55:04 2008''

Revision as of 12:55, 20 March 2008


PDB ID 1wc6

Drag the structure with the mouse to rotate
, resolution 2.51Å
Sites:
Ligands: and
Activity: Adenylate cyclase, with EC number 4.6.1.1
Coordinates: save as pdb, mmCIF, xml



SOLUBLE ADENYLYL CYCLASE CYAC FROM S. PLATENSIS IN COMPLEX WITH RP-ATPALPHAS IN PRESENCE OF BICARBONATE


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.

About this Structure

1WC6 is a Single protein structure of sequence from Arthrospira platensis. Full crystallographic information is available from OCA.

Reference

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

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