4f1h
From Proteopedia
(Difference between revisions)
m (Protected "4f1h" [edit=sysop:move=sysop]) |
|||
(8 intermediate revisions not shown.) | |||
Line 1: | Line 1: | ||
- | '''Unreleased structure''' | ||
- | + | ==Crystal structure of TDP2 from Danio rerio complexed with a single strand DNA== | |
+ | <StructureSection load='4f1h' size='340' side='right'caption='[[4f1h]], [[Resolution|resolution]] 1.66Å' scene=''> | ||
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[4f1h]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Danio_rerio Danio rerio]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4F1H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4F1H 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]] 1.662Å</td></tr> | ||
+ | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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=4f1h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4f1h OCA], [https://pdbe.org/4f1h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4f1h RCSB], [https://www.ebi.ac.uk/pdbsum/4f1h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4f1h ProSAT]</span></td></tr> | ||
+ | </table> | ||
+ | == Function == | ||
+ | [https://www.uniprot.org/uniprot/TYDP2_DANRE TYDP2_DANRE] DNA repair enzyme that can remove a variety of covalent adducts from DNA through hydrolysis of a 5'-phosphodiester bond, giving rise to DNA with a free 5' phosphate. Catalyzes the hydrolysis of dead-end complexes between DNA and the topoisomerase 2 (top2) active site tyrosine residue. Hydrolyzes 5'-phosphoglycolates on protruding 5' ends on DNA double-strand breaks (DSBs) due to DNA damage by radiation and free radicals (By similarity). Controls gastrulation movements and left/right (L/R) axis determination via smad3-mediated regulation of cdh1/e-cadherin. Regulates the formation of Kupffer's vesicle, a signaling center essential for establishing L/R asymmetry. Modulates smad3 activity through modulating nodal-acvr1/akt4 signaling.<ref>PMID:18039968</ref> | ||
- | + | ==See Also== | |
- | + | *[[Phosphodiesterase 3D structures|Phosphodiesterase 3D structures]] | |
- | + | == References == | |
+ | <references/> | ||
+ | __TOC__ | ||
+ | </StructureSection> | ||
+ | [[Category: Danio rerio]] | ||
+ | [[Category: Large Structures]] | ||
+ | [[Category: Aihara H]] | ||
+ | [[Category: Kurahashi K]] | ||
+ | [[Category: Shi K]] |
Current revision
Crystal structure of TDP2 from Danio rerio complexed with a single strand DNA
|