View source for 6yp4


==Putative adenylyl cyclase HpAC1 from Hippeastrum reveals a dominant triphophatase activity==
<StructureSection load='6yp4' size='340' side='right'caption='[[6yp4]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6yp4]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Hippeastrum_hybrid_cultivar Hippeastrum hybrid cultivar]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6YP4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6YP4 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]] 1.945411&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GCP:PHOSPHOMETHYLPHOSPHONIC+ACID+GUANYLATE+ESTER'>GCP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=6yp4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6yp4 OCA], [https://pdbe.org/6yp4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6yp4 RCSB], [https://www.ebi.ac.uk/pdbsum/6yp4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6yp4 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/E1AQY1_9ASPA E1AQY1_9ASPA] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
HpAC1, a protein from Hippeastrum hybrid cultivars, was previously suggested to be a plant adenylyl cyclase. We describe a structural and enzymatic characterization of HpAC1. A crystal structure of HpAC1 in complex with a non-hydrolyzable GTP analog confirms a generic CYTH architecture, comprising a beta-barrel with an internal substrate site. The structure reveals significant active site differences to AC proteins with CYTH fold, however, and we find that HpAC1 lacks measurable AC activity. Instead, HpAC1 has substantial triphosphatase activity, indicating this protective activity or a related activity as the protein's physiological function.

Crystal structure and enzymatic characterization of the putative adenylyl cyclase HpAC1 from Hippeastrum reveal dominant triphosphatase activity.,Kleinboelting S, Miehling J, Steegborn C J Struct Biol. 2020 Oct 16;212(3):107649. doi: 10.1016/j.jsb.2020.107649. PMID:33075486<ref>PMID:33075486</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6yp4" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Hippeastrum hybrid cultivar]]
[[Category: Large Structures]]
[[Category: Kleinboelting S]]
[[Category: Steegborn C]]