1wc5: Difference between revisions

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-[[Image:1wc5.png|left|200px]]
-<!--
+==Soluble adenylyl cyclase CyaC from S. platensis in complex with alpha, beta-methylene-ATP in presence of bicarbonate==
-The line below this paragraph, containing "STRUCTURE_1wc5", creates the "Structure Box" on the page.
+<StructureSection load='1wc5' size='340' side='right'caption='[[1wc5]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[1wc5]] 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=1WC5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1WC5 FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</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>
--->
+<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=MG:MAGNESIUM+ION'>MG</scene></td></tr>
-{{STRUCTURE_1wc5|  PDB=1wc5  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1wc5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wc5 OCA], [https://pdbe.org/1wc5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1wc5 RCSB], [https://www.ebi.ac.uk/pdbsum/1wc5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1wc5 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/O32393_ARTPT O32393_ARTPT]
+== 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/wc/1wc5_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=1wc5 ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+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.
-===SOLUBLE ADENYLYL CYCLASE CYAC FROM S. PLATENSIS IN COMPLEX WITH ALPHA,BETA-METHYLENE-ATP IN PRESENCE OF BICARBONATE===
+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>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-<!--
+</div>
-The line below this paragraph, {{ABSTRACT_PUBMED_15619637}}, adds the Publication Abstract to the page
+<div class="pdbe-citations 1wc5" style="background-color:#fffaf0;"></div>
-(as it appears on PubMed at http://www.pubmed.gov), where 15619637 is the PubMed ID number.
--->
-{{ABSTRACT_PUBMED_15619637}}
-==About this Structure==
-[[1wc5]] is a 4 chain structure of [[Adenylyl cyclase]] with 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=1WC5 OCA].
 ==See Also==
-*[[Adenylyl cyclase]]
+*[[3D Adenylyl cyclase 3D structures|3D Adenylyl cyclase 3D structures]]
+== References ==
-==Reference==
+<references/>
-<ref group="xtra">PMID:15619637</ref><references group="xtra"/>
+__TOC__
-[[Category: Adenylate cyclase]]
+</StructureSection>
 [[Category: Arthrospira platensis]]
-[[Category: Buck, J.]]
+[[Category: Large Structures]]
-[[Category: Levin, L R.]]
+[[Category: Buck J]]
-[[Category: Litvin, T N.]]
+[[Category: Levin LR]]
-[[Category: Steegborn, C.]]
+[[Category: Litvin TN]]
-[[Category: Wu, H.]]
+[[Category: Steegborn C]]
-[[Category: Camp signaling]]
+[[Category: Wu H]]
-[[Category: Cyclase]]
-[[Category: Lyase]]
-[[Category: Soluble adenylyl cyclase]]