2j08
From Proteopedia
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| - | [[Image:2j08.jpg|left|200px]] | ||
| - | + | ==Thermus DNA photolyase with 8-Iod-riboflavin antenna chromophore== | |
| - | + | <StructureSection load='2j08' size='340' side='right'caption='[[2j08]], [[Resolution|resolution]] 2.61Å' scene=''> | |
| - | You may | + | == Structural highlights == |
| - | + | <table><tr><td colspan='2'>[[2j08]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_thermophilus_HB8 Thermus thermophilus HB8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2J08 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2J08 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]] 2.61Å</td></tr> | |
| - | -- | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=IRF:1-DEOXY-1-(8-IODO-7-METHYL-2,4-DIOXO-3,4-DIHYDROBENZO[G]PTERIDIN-10(2H)-YL)-D-RIBITOL'>IRF</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=2j08 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2j08 OCA], [https://pdbe.org/2j08 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2j08 RCSB], [https://www.ebi.ac.uk/pdbsum/2j08 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2j08 ProSAT]</span></td></tr> | |
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/PHR_THET8 PHR_THET8] Involved in repair of UV radiation-induced DNA damage. Catalyzes the light-dependent monomerization (300-600 nm) of cyclobutyl pyrimidine dimers (in cis-syn configuration), which are formed between adjacent bases on the same DNA strand upon exposure to ultraviolet radiation (By similarity). | ||
| + | == Evolutionary Conservation == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/j0/2j08_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2j08 ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | X-ray crystallographic and functional analysis of the class I DNA photolyase from Thermus thermophilus revealed the binding of flavin mononucleotide (FMN) as an antenna chromophore. The binding mode of FMN closely coincides with the binding of a deazaflavin-like chromophore in the related class I DNA photolyase from Anacystis nidulans. Compared to the R46E mutant, which lacks a conserved arginine in the binding site for the antenna chromophore, the FMN-comprising holophotolyase exhibits an eightfold higher activity at 450 nm. The facile incorporation of the flavin cofactors 8-hydroxy-deazariboflavin and 8-iodo-8-demethyl-riboflavin into the binding site for the antenna chromophore paves the way for wavelength-tuning of the activity spectra of DNA photolyases by using synthetic flavins. | ||
| - | + | Natural and non-natural antenna chromophores in the DNA photolyase from Thermus thermophilus.,Klar T, Kaiser G, Hennecke U, Carell T, Batschauer A, Essen LO Chembiochem. 2006 Nov;7(11):1798-806. PMID:17051659<ref>PMID:17051659</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 2j08" style="background-color:#fffaf0;"></div> | |
| - | + | == References == | |
| - | [[Category: | + | <references/> |
| - | [[Category: Thermus thermophilus]] | + | __TOC__ |
| - | [[Category: Batschauer | + | </StructureSection> |
| - | [[Category: Carell | + | [[Category: Large Structures]] |
| - | [[Category: Essen | + | [[Category: Thermus thermophilus HB8]] |
| - | [[Category: Hennecke | + | [[Category: Batschauer A]] |
| - | [[Category: Kaiser | + | [[Category: Carell T]] |
| - | [[Category: Klar | + | [[Category: Essen L-O]] |
| - | + | [[Category: Hennecke U]] | |
| - | + | [[Category: Kaiser G]] | |
| - | + | [[Category: Klar T]] | |
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Current revision
Thermus DNA photolyase with 8-Iod-riboflavin antenna chromophore
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