|
|
| Line 3: |
Line 3: |
| | <StructureSection load='5hee' size='340' side='right'caption='[[5hee]], [[Resolution|resolution]] 1.41Å' scene=''> | | <StructureSection load='5hee' size='340' side='right'caption='[[5hee]], [[Resolution|resolution]] 1.41Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5hee]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Pyrococcus_kodakaraensis_(strain_kod1) Pyrococcus kodakaraensis (strain kod1)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5HEE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5HEE FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5hee]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermococcus_kodakarensis_KOD1 Thermococcus kodakarensis KOD1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5HEE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5HEE FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.41Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TK2203 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=69014 Pyrococcus kodakaraensis (strain KOD1)])</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=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=5hee FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hee OCA], [http://pdbe.org/5hee PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5hee RCSB], [http://www.ebi.ac.uk/pdbsum/5hee PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5hee ProSAT]</span></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=5hee FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hee OCA], [https://pdbe.org/5hee PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5hee RCSB], [https://www.ebi.ac.uk/pdbsum/5hee PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5hee ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q5JHM2_THEKO Q5JHM2_THEKO] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 22: |
Line 24: |
| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Miki, K]] | + | [[Category: Thermococcus kodakarensis KOD1]] |
| - | [[Category: Nishitani, Y]] | + | [[Category: Miki K]] |
| - | [[Category: Dioxygenase]] | + | [[Category: Nishitani Y]] |
| - | [[Category: Oxidoreductase]]
| + | |
| - | [[Category: Putative]]
| + | |
| Structural highlights
Function
Q5JHM2_THEKO
Publication Abstract from PubMed
The TK2203 protein from the hyperthermophilic archaeon Thermococcus kodakarensis KOD1 (262 residues, 29 kDa) is a putative extradiol dioxygenase catalyzing the cleavage of C-C bonds in catechol derivatives. It contains three metal-binding residues, but has no significant sequence similarity to proteins for which structures have been determined. Here, the first crystal structure of the TK2203 protein was determined at 1.41 A resolution to investigate its functional role. Structure analysis reveals that this protein shares the same fold and catalytic residues as other extradiol dioxygenases, strongly suggesting the same enzymatic activity. Furthermore, the important region contributing to substrate selectivity is discussed.
Crystal structure of the TK2203 protein from Thermococcus kodakarensis, a putative extradiol dioxygenase.,Nishitani Y, Simons JR, Kanai T, Atomi H, Miki K Acta Crystallogr F Struct Biol Commun. 2016 Jun 1;72(Pt 6):427-33. doi:, 10.1107/S2053230X16006920. Epub 2016 May 23. PMID:27303894[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Nishitani Y, Simons JR, Kanai T, Atomi H, Miki K. Crystal structure of the TK2203 protein from Thermococcus kodakarensis, a putative extradiol dioxygenase. Acta Crystallogr F Struct Biol Commun. 2016 Jun 1;72(Pt 6):427-33. doi:, 10.1107/S2053230X16006920. Epub 2016 May 23. PMID:27303894 doi:http://dx.doi.org/10.1107/S2053230X16006920
|
