1ab8: Difference between revisions

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New page: left|200px<br /><applet load="1ab8" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ab8, resolution 2.2Å" /> '''RAT TYPE II ADENYLYL ...
 
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[[Image:1ab8.gif|left|200px]]<br /><applet load="1ab8" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1ab8.gif|left|200px]]<br /><applet load="1ab8" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1ab8, resolution 2.2&Aring;" />
caption="1ab8, resolution 2.2&Aring;" />
'''RAT TYPE II ADENYLYL CYCLASE C2 DOMAIN/FORSKOLIN COMPLEX'''<br />
'''RAT TYPE II ADENYLYL CYCLASE C2 DOMAIN/FORSKOLIN COMPLEX'''<br />


==Overview==
==Overview==
Mammalian adenylyl cyclases contain two conserved regions, C1 and C2, which are responsible for forskolin- and G-protein-stimulated catalysis., The structure of the C2 catalytic region of type II rat adenylyl cyclase, has an alpha/beta class fold in a wreath-like dimer, which has a central, cleft. Two forskolin molecules bind in hydrophobic pockets at the ends of, cleft. The central part of the cleft is lined by charged residues, implicated in ATP binding. Forskolin appears to activate adenylyl cyclase, by promoting the assembly of the active dimer and by direct interaction, within the catalytic cleft. Other adenylyl cyclase regulators act at the, dimer interface or on a flexible C-terminal region.
Mammalian adenylyl cyclases contain two conserved regions, C1 and C2, which are responsible for forskolin- and G-protein-stimulated catalysis. The structure of the C2 catalytic region of type II rat adenylyl cyclase has an alpha/beta class fold in a wreath-like dimer, which has a central cleft. Two forskolin molecules bind in hydrophobic pockets at the ends of cleft. The central part of the cleft is lined by charged residues implicated in ATP binding. Forskolin appears to activate adenylyl cyclase by promoting the assembly of the active dimer and by direct interaction within the catalytic cleft. Other adenylyl cyclase regulators act at the dimer interface or on a flexible C-terminal region.


==About this Structure==
==About this Structure==
1AB8 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with FOK as [http://en.wikipedia.org/wiki/ligand ligand]. 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=1AB8 OCA].  
1AB8 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with <scene name='pdbligand=FOK:'>FOK</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. 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=1AB8 OCA].  


==Reference==
==Reference==
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[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Hurley, J.H.]]
[[Category: Hurley, J H.]]
[[Category: Zhang, G.]]
[[Category: Zhang, G.]]
[[Category: FOK]]
[[Category: FOK]]
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[[Category: plasmid]]
[[Category: plasmid]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 10:44:02 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:42:47 2008''

Revision as of 12:42, 21 February 2008

File:1ab8.gif


1ab8, resolution 2.2Å

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RAT TYPE II ADENYLYL CYCLASE C2 DOMAIN/FORSKOLIN COMPLEX

OverviewOverview

Mammalian adenylyl cyclases contain two conserved regions, C1 and C2, which are responsible for forskolin- and G-protein-stimulated catalysis. The structure of the C2 catalytic region of type II rat adenylyl cyclase has an alpha/beta class fold in a wreath-like dimer, which has a central cleft. Two forskolin molecules bind in hydrophobic pockets at the ends of cleft. The central part of the cleft is lined by charged residues implicated in ATP binding. Forskolin appears to activate adenylyl cyclase by promoting the assembly of the active dimer and by direct interaction within the catalytic cleft. Other adenylyl cyclase regulators act at the dimer interface or on a flexible C-terminal region.

About this StructureAbout this Structure

1AB8 is a Single protein structure of sequence from Rattus norvegicus with as ligand. Active as Adenylate cyclase, with EC number 4.6.1.1 Full crystallographic information is available from OCA.

ReferenceReference

Structure of the adenylyl cyclase catalytic core., Zhang G, Liu Y, Ruoho AE, Hurley JH, Nature. 1997 Mar 20;386(6622):247-53. PMID:9069282

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