6aek: Difference between revisions
From Proteopedia
Jump to navigationJump to search
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
==Crystal structure of ENPP1 in complex with pApG== | |||
<StructureSection load='6aek' size='340' side='right' caption='[[6aek]], [[Resolution|resolution]] 1.80Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6aek]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6AEK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6AEK FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6aek FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6aek OCA], [http://pdbe.org/6aek PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6aek RCSB], [http://www.ebi.ac.uk/pdbsum/6aek PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6aek ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
ENPP1 (Ecto-nucleotide pyrophosphatase phosphodiesterase 1), a type II transmembrane glycoprotein, hydrolyzes ATP to produce AMP and diphosphate, thereby inhibiting bone mineralization. A recent study showed that ENPP1 also preferentially hydrolyzes 2'3'-cGAMP (cyclic GMP-AMP) but not its linkage isomer 3'3'-cGAMP, and negatively regulates the cGAS-STING pathway in the innate immune system. Here, we present the high-resolution crystal structures of ENPP1 in complex with 3'3'-cGAMP and the reaction intermediate pA(3',5')pG. The structures revealed that the adenine and guanine bases of the dinucleotides are recognized by nucleotide- and guanine-pockets, respectively. Furthermore, the structures indicate that 2'3'-cGAMP, but not 3'3'-cGAMP, binds to the active site in a conformation suitable for catalysis, thereby explaining the specific degradation of 2'3'-cGAMP by ENPP1. Our findings provide insights into how ENPP1 hydrolyzes both ATP and cGAMP to participate in the two distinct biological processes. | |||
Structural insights into cGAMP degradation by Ecto-nucleotide pyrophosphatase phosphodiesterase 1.,Kato K, Nishimasu H, Oikawa D, Hirano S, Hirano H, Kasuya G, Ishitani R, Tokunaga F, Nureki O Nat Commun. 2018 Oct 24;9(1):4424. doi: 10.1038/s41467-018-06922-7. PMID:30356045<ref>PMID:30356045</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 6aek" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Hirano, H]] | [[Category: Hirano, H]] | ||
[[Category: Hirano, S]] | [[Category: Hirano, S]] | ||
[[Category: Ishitani, R]] | |||
[[Category: Kato, K]] | [[Category: Kato, K]] | ||
[[Category: Nishimasu, H]] | [[Category: Nishimasu, H]] | ||
[[Category: | [[Category: Nureki, O]] | ||
[[Category: Cgamp]] | |||
[[Category: Cgas-sting]] | |||
[[Category: Cyclic gmp-amp]] | |||
[[Category: Enzyme]] | |||
[[Category: Immunosuppressant]] | |||
[[Category: Phoshodiesterase]] | |||
Revision as of 07:24, 6 March 2019
Crystal structure of ENPP1 in complex with pApG
| ||||||||||||
