1wc4

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[[Image:1wc4.gif|left|200px]]<br />
 
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<applet load="1wc4" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1wc4, resolution 3.00&Aring;" />
 
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'''SOLUBLE ADENYLYL CYCLASE CYAC FROM S. PLATENSIS IN COMPLEX WITH ALPHA,BETA-METHYLENE-ATP AND EUROPIUM'''<br />
 
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==Overview==
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==Soluble adenylyl cyclase CyaC from S. platensis in complex with alpha, beta-methylene-ATP and Europium==
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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.
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<StructureSection load='1wc4' size='340' side='right'caption='[[1wc4]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1wc4]] is a 2 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=1WC4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1WC4 FirstGlance]. <br>
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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]] 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=EU3:EUROPIUM+(III)+ION'>EU3</scene></td></tr>
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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=1wc4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wc4 OCA], [https://pdbe.org/1wc4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1wc4 RCSB], [https://www.ebi.ac.uk/pdbsum/1wc4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1wc4 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/wc/1wc4_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=1wc4 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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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.
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==About this Structure==
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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:15619637<ref>PMID:15619637</ref>
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1WC4 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 EU3 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] Structure known Active Site: AC1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1WC4 OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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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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</div>
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[[Category: Adenylate cyclase]]
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<div class="pdbe-citations 1wc4" style="background-color:#fffaf0;"></div>
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[[Category: Arthrospira platensis]]
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[[Category: Single protein]]
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[[Category: Buck, J.]]
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[[Category: Levin, L.R.]]
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[[Category: Litvin, T.N.]]
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[[Category: Steegborn, C.]]
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[[Category: Wu, H.]]
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[[Category: APC]]
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[[Category: EU3]]
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[[Category: camp signaling]]
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[[Category: cyclase]]
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[[Category: lyase]]
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[[Category: soluble adenylyl cyclase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 17:31:57 2007''
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==See Also==
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*[[3D Adenylyl cyclase 3D structures|3D Adenylyl cyclase 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Arthrospira platensis]]
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[[Category: Large Structures]]
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[[Category: Buck J]]
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[[Category: Levin LR]]
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[[Category: Litvin TN]]
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[[Category: Steegborn C]]
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[[Category: Wu H]]

Current revision

Soluble adenylyl cyclase CyaC from S. platensis in complex with alpha, beta-methylene-ATP and Europium

PDB ID 1wc4

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