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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"
caption="1ab8, resolution 2.2&Aring;" />
'''RAT TYPE II ADENYLYL CYCLASE C2 DOMAIN/FORSKOLIN COMPLEX'''<br />


==Overview==
==RAT TYPE II ADENYLYL CYCLASE C2 DOMAIN/FORSKOLIN COMPLEX==
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.
<StructureSection load='1ab8' size='340' side='right'caption='[[1ab8]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1ab8]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AB8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AB8 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FOK:FORSKOLIN'>FOK</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ab8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ab8 OCA], [https://pdbe.org/1ab8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ab8 RCSB], [https://www.ebi.ac.uk/pdbsum/1ab8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ab8 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/ADCY2_RAT ADCY2_RAT] This is a membrane-bound, calmodulin-insensitive adenylyl cyclase.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ab/1ab8_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1ab8 ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
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].
*[[3D Adenylyl cyclase 3D structures|3D Adenylyl cyclase 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
Structure of the adenylyl cyclase catalytic core., Zhang G, Liu Y, Ruoho AE, Hurley JH, Nature. 1997 Mar 20;386(6622):247-53. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9069282 9069282]
[[Category: Large Structures]]
[[Category: Adenylate cyclase]]
[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
[[Category: Single protein]]
[[Category: Hurley JH]]
[[Category: Hurley, J.H.]]
[[Category: Zhang G]]
[[Category: Zhang, G.]]
[[Category: FOK]]
[[Category: adenylyl cyclase]]
[[Category: complex (transferase/inhibitor)]]
[[Category: lyase]]
[[Category: plasmid]]
 
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