2bw7

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[[Image:2bw7.gif|left|200px]]
 
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==A novel mechanism for adenylyl cyclase inhibition from the crystal structure of its complex with catechol estrogen==
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The line below this paragraph, containing "STRUCTURE_2bw7", creates the "Structure Box" on the page.
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<StructureSection load='2bw7' size='340' side='right'caption='[[2bw7]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[2bw7]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Arthrospira_platensis Arthrospira platensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BW7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BW7 FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=APC:DIPHOSPHOMETHYLPHOSPHONIC+ACID+ADENOSYL+ESTER'>APC</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=ECS:2,3,17BETA-TRIHYDROXY-1,3,5(10)-ESTRATRIENE'>ECS</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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{{STRUCTURE_2bw7| PDB=2bw7 | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2bw7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bw7 OCA], [https://pdbe.org/2bw7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2bw7 RCSB], [https://www.ebi.ac.uk/pdbsum/2bw7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2bw7 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/O32393_ARTPT O32393_ARTPT]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bw/2bw7_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=2bw7 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Catechol estrogens are steroid metabolites that elicit physiological responses through binding to a variety of cellular targets. We show here that catechol estrogens directly inhibit soluble adenylyl cyclases and the abundant trans-membrane adenylyl cyclases. Catechol estrogen inhibition is non-competitive with respect to the substrate ATP, and we solved the crystal structure of a catechol estrogen bound to a soluble adenylyl cyclase from Spirulina platensis in complex with a substrate analog. The catechol estrogen is bound to a newly identified, conserved hydrophobic patch near the active center but distinct from the ATP-binding cleft. Inhibitor binding leads to a chelating interaction between the catechol estrogen hydroxyl groups and the catalytic magnesium ion, distorting the active site and trapping the enzyme substrate complex in a non-productive conformation. This novel inhibition mechanism likely applies to other adenylyl cyclase inhibitors, and the identified ligand-binding site has important implications for the development of specific adenylyl cyclase inhibitors.
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'''A NOVEL MECHANISM FOR ADENYLYL CYCLASE INHIBITION FROM THE CRYSTAL STRUCTURE OF ITS COMPLEX WITH CATECHOL ESTROGEN'''
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A novel mechanism for adenylyl cyclase inhibition from the crystal structure of its complex with catechol estrogen.,Steegborn C, Litvin TN, Hess KC, Capper AB, Taussig R, Buck J, Levin LR, Wu H J Biol Chem. 2005 Sep 9;280(36):31754-9. Epub 2005 Jul 7. PMID:16002394<ref>PMID:16002394</ref>
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==Overview==
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Catechol estrogens are steroid metabolites that elicit physiological responses through binding to a variety of cellular targets. We show here that catechol estrogens directly inhibit soluble adenylyl cyclases and the abundant trans-membrane adenylyl cyclases. Catechol estrogen inhibition is non-competitive with respect to the substrate ATP, and we solved the crystal structure of a catechol estrogen bound to a soluble adenylyl cyclase from Spirulina platensis in complex with a substrate analog. The catechol estrogen is bound to a newly identified, conserved hydrophobic patch near the active center but distinct from the ATP-binding cleft. Inhibitor binding leads to a chelating interaction between the catechol estrogen hydroxyl groups and the catalytic magnesium ion, distorting the active site and trapping the enzyme substrate complex in a non-productive conformation. This novel inhibition mechanism likely applies to other adenylyl cyclase inhibitors, and the identified ligand-binding site has important implications for the development of specific adenylyl cyclase inhibitors.
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==About this Structure==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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2BW7 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=2BW7 OCA].
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</div>
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<div class="pdbe-citations 2bw7" style="background-color:#fffaf0;"></div>
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==Reference==
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==See Also==
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A novel mechanism for adenylyl cyclase inhibition from the crystal structure of its complex with catechol estrogen., Steegborn C, Litvin TN, Hess KC, Capper AB, Taussig R, Buck J, Levin LR, Wu H, J Biol Chem. 2005 Sep 9;280(36):31754-9. Epub 2005 Jul 7. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16002394 16002394]
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*[[3D Adenylyl cyclase 3D structures|3D Adenylyl cyclase 3D structures]]
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[[Category: Adenylate cyclase]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Arthrospira platensis]]
[[Category: Arthrospira platensis]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Buck, J.]]
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[[Category: Buck J]]
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[[Category: Capper, A B.]]
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[[Category: Capper AB]]
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[[Category: Hess, K C.]]
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[[Category: Hess KC]]
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[[Category: Levin, L R.]]
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[[Category: Levin LR]]
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[[Category: Litvin, T N.]]
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[[Category: Litvin TN]]
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[[Category: Steegborn, C.]]
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[[Category: Steegborn C]]
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[[Category: Taussig, R.]]
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[[Category: Taussig R]]
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[[Category: Wu, H.]]
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[[Category: Wu H]]
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[[Category: Adenylyl cyclase]]
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[[Category: Camp signaling]]
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[[Category: Catechol estrogen]]
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[[Category: Inhibitor complex]]
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[[Category: Oxidoreductase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 20:53:22 2008''
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Current revision

A novel mechanism for adenylyl cyclase inhibition from the crystal structure of its complex with catechol estrogen

PDB ID 2bw7

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