View source for 5oyh


==crystal structure of the catalytic core of a rhodopsin-guanylyl cyclase with converted specificity in complex with ATPalphaS==
<StructureSection load='5oyh' size='340' side='right'caption='[[5oyh]], [[Resolution|resolution]] 2.25&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5oyh]] is a 16 chain structure with sequence from [https://en.wikipedia.org/wiki/Catenaria_anguillulae_PL171 Catenaria anguillulae PL171]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5OYH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5OYH 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]] 2.249&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=T99:ADENOSINE-5-SP-ALPHA-THIO-TRIPHOSPHATE'>T99</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=5oyh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5oyh OCA], [https://pdbe.org/5oyh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5oyh RCSB], [https://www.ebi.ac.uk/pdbsum/5oyh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5oyh ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A1Y2HEJ3_9FUNG A0A1Y2HEJ3_9FUNG] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The cyclic nucleotides cAMP and cGMP are important second messengers that orchestrate fundamental cellular responses. Here, we present the characterization of the rhodopsin-guanylyl cyclase from Catenaria anguillulae (CaRhGC), which produces cGMP in response to green light with a light to dark activity ratio &gt;1000. After light excitation the putative signaling state forms with tau = 31 ms and decays with tau = 570 ms. Mutations (up to 6) within the nucleotide binding site generate rhodopsin-adenylyl cyclases (CaRhACs) of which the double mutated YFP-CaRhAC (E497K/C566D) is the most suitable for rapid cAMP production in neurons. Furthermore, the crystal structure of the ligand-bound AC domain (2.25 A) reveals detailed information about the nucleotide binding mode within this recently discovered class of enzyme rhodopsin. Both YFP-CaRhGC and YFP-CaRhAC are favorable optogenetic tools for non-invasive, cell-selective, and spatio-temporally precise modulation of cAMP/cGMP with light.

Rhodopsin-cyclases for photocontrol of cGMP/cAMP and 2.3 A structure of the adenylyl cyclase domain.,Scheib U, Broser M, Constantin OM, Yang S, Gao S, Mukherjee S, Stehfest K, Nagel G, Gee CE, Hegemann P Nat Commun. 2018 May 24;9(1):2046. doi: 10.1038/s41467-018-04428-w. PMID:29799525<ref>PMID:29799525</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5oyh" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Catenaria anguillulae PL171]]
[[Category: Large Structures]]
[[Category: Broser M]]
[[Category: Hegemann P]]
[[Category: Scheib U]]