2ypc: Difference between revisions
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==Catalytic domain of mouse 2',3'-cyclic nucleotide 3'- phosphodiesterase, with mutation H309S, crystallized with 2',3-(SP)-Cyclic-AMPS== | ==Catalytic domain of mouse 2',3'-cyclic nucleotide 3'- phosphodiesterase, with mutation H309S, crystallized with 2',3-(SP)-Cyclic-AMPS== | ||
<StructureSection load='2ypc' size='340' side='right' caption='[[2ypc]], [[Resolution|resolution]] 1.89Å' scene=''> | <StructureSection load='2ypc' size='340' side='right'caption='[[2ypc]], [[Resolution|resolution]] 1.89Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2ypc]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[2ypc]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2YPC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2YPC FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=QQX:[(3AR,4R,6R,6AR)-4-(6-AMINOPURIN-9-YL)-2-OXIDANYL-2-SULFANYLIDENE-3A,4,6,6A-TETRAHYDROFURO[3,4-D][1,3,2]DIOXAPHOSPHOL-6-YL]METHANOL'>QQX</scene | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.894Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=QQX:[(3AR,4R,6R,6AR)-4-(6-AMINOPURIN-9-YL)-2-OXIDANYL-2-SULFANYLIDENE-3A,4,6,6A-TETRAHYDROFURO[3,4-D][1,3,2]DIOXAPHOSPHOL-6-YL]METHANOL'>QQX</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=2ypc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ypc OCA], [https://pdbe.org/2ypc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ypc RCSB], [https://www.ebi.ac.uk/pdbsum/2ypc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ypc ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/CN37_MOUSE CN37_MOUSE] May participate in RNA metabolism in the myelinating cell, CNP is the third most abundant protein in central nervous system myelin.<ref>PMID:22393399</ref> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
| Line 22: | Line 21: | ||
==See Also== | ==See Also== | ||
*[[Phosphodiesterase|Phosphodiesterase]] | *[[Phosphodiesterase 3D structures|Phosphodiesterase 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Mus musculus]] | ||
[[Category: Han | [[Category: Han H]] | ||
[[Category: Kursula | [[Category: Kursula P]] | ||
[[Category: Lehtimaki | [[Category: Lehtimaki M]] | ||
[[Category: Myllykoski | [[Category: Myllykoski M]] | ||
[[Category: Raasakka | [[Category: Raasakka A]] | ||
Latest revision as of 16:38, 30 August 2023
Catalytic domain of mouse 2',3'-cyclic nucleotide 3'- phosphodiesterase, with mutation H309S, crystallized with 2',3-(SP)-Cyclic-AMPSCatalytic domain of mouse 2',3'-cyclic nucleotide 3'- phosphodiesterase, with mutation H309S, crystallized with 2',3-(SP)-Cyclic-AMPS
Structural highlights
FunctionCN37_MOUSE May participate in RNA metabolism in the myelinating cell, CNP is the third most abundant protein in central nervous system myelin.[1] Publication Abstract from PubMed2H phosphoesterases catalyze reactions on nucleotide substrates and contain two conserved histidine residues in the active site. Very limited information is currently available on the details of the active site and substrate/product binding during the catalytic cycle of these enzymes. We performed a comprehensive X-ray crystallographic study of mouse 2',3'-cyclic nucleotide 3'-phosphodiesterase (CNPase), a membrane-associated enzyme present at high levels in the tetrapod myelin sheath. We determined crystal structures of the CNPase phosphodiesterase domain complexed with substrate, product, and phosphorothioate analogues. The data provide detailed information on the CNPase reaction mechanism, including substrate binding mode and coordination of the nucleophilic water molecule. Linked to the reaction, an open/close motion of the beta5-alpha7 loop is observed. The role of the N terminus of helix alpha7 - unique for CNPase in the 2H family - during the reaction indicates that 2H phosphoesterases differ in their respective reaction mechanisms, despite the conserved catalytic residues. Furthermore, based on small-angle X-ray scattering, we present a model for the full-length enzyme, indicating the two domains of CNPase form an elongated molecule. Finally, based on our structural data and a comprehensive bioinformatics study, we discuss the conservation of CNPase in various organisms. Crystallographic analysis of the reaction cycle of 2',3'-cyclic nucleotide 3'-phosphodiesterase, a unique member of the 2H phosphoesterase family.,Myllykoski M, Raasakka A, Lehtimaki M, Han H, Kursula I, Kursula P J Mol Biol. 2013 Jul 2. pii: S0022-2836(13)00391-4. doi:, 10.1016/j.jmb.2013.06.012. PMID:23831225[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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