5hzt
From Proteopedia
(Difference between revisions)
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<StructureSection load='5hzt' size='340' side='right' caption='[[5hzt]], [[Resolution|resolution]] 2.84Å' scene=''> | <StructureSection load='5hzt' size='340' side='right' caption='[[5hzt]], [[Resolution|resolution]] 2.84Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[5hzt]] is a 12 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5HZT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5HZT FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5hzt]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/Echinophyllia_sp._sc22 Echinophyllia sp. sc22]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5HZT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5HZT FirstGlance]. <br> |
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene></td></tr> | ||
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=GYS:[(4Z)-2-(1-AMINO-2-HYDROXYETHYL)-4-(4-HYDROXYBENZYLIDENE)-5-OXO-4,5-DIHYDRO-1H-IMIDAZOL-1-YL]ACETIC+ACID'>GYS</scene></td></tr> | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=GYS:[(4Z)-2-(1-AMINO-2-HYDROXYETHYL)-4-(4-HYDROXYBENZYLIDENE)-5-OXO-4,5-DIHYDRO-1H-IMIDAZOL-1-YL]ACETIC+ACID'>GYS</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2gx2|2gx2]], [[5hzu|5hzu]], [[5hzs|5hzs]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2gx2|2gx2]], [[5hzu|5hzu]], [[5hzs|5hzs]]</td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Dronpa ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=301887 Echinophyllia sp. SC22])</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=5hzt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hzt OCA], [http://pdbe.org/5hzt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5hzt RCSB], [http://www.ebi.ac.uk/pdbsum/5hzt PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5hzt ProSAT]</span></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=5hzt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hzt OCA], [http://pdbe.org/5hzt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5hzt RCSB], [http://www.ebi.ac.uk/pdbsum/5hzt PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5hzt ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Many fluorescent proteins (FPs) show fluorescence quenching by specific metal ions, which can be applied towards metal biosensor development. In this study, we investigated the significant fluorescence quenching of Dronpa by Co(2+) and Cu(2+) ions. Crystal structures of Co(2+) -, Ni(2+) - and Cu(2+) -bound Dronpa revealed previously unseen, unique, metal-binding sites for fluorescence quenching. These metal ions commonly interact with surface-exposed histidine residues (His194-His210 and His210-His212), and interact indirectly with chromophores. Structural analysis of the Co(2+) - and Cu(2+) - binding sites of Dronpa provides insight into FP-based metal biosensor engineering. | ||
| + | |||
| + | Crystal structures of Dronpa complexed with quenchable metal ions provide insight into metal biosensor development.,Kim IJ, Kim S, Park J, Eom I, Kim S, Kim JH, Ha SC, Kim YG, Hwang KY, Nam KH FEBS Lett. 2016 Sep;590(17):2982-90. doi: 10.1002/1873-3468.12316. Epub 2016 Jul , 30. PMID:27433793<ref>PMID:27433793</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 5hzt" style="background-color:#fffaf0;"></div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[Dronpa|Dronpa]] | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Echinophyllia sp. sc22]] | ||
[[Category: Hwang, K Y]] | [[Category: Hwang, K Y]] | ||
[[Category: Nam, K H]] | [[Category: Nam, K H]] | ||
[[Category: Fluorescent protein]] | [[Category: Fluorescent protein]] | ||
[[Category: Luminescent protein]] | [[Category: Luminescent protein]] | ||
Revision as of 20:41, 2 December 2018
Crystal structure of Dronpa-Cu2+
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