1owp

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(New page: 200px<br /><applet load="1owp" size="450" color="white" frame="true" align="right" spinBox="true" caption="1owp, resolution 2.30&Aring;" /> '''DATA6:photoreduced D...)
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[[Image:1owp.jpg|left|200px]]<br /><applet load="1owp" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1owp, resolution 2.30&Aring;" />
 
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'''DATA6:photoreduced DNA pholyase / received X-rays dose 4.8 exp15 photons/mm2'''<br />
 
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==Overview==
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==DATA6:photoreduced DNA pholyase / received X-rays dose 4.8 exp15 photons/mm2==
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DNA photolyase is a unique flavoenzyme that repairs UV-induced DNA lesions, using the energy of visible light. Anacystis nidulans photolyase contains, a light-harvesting chromophore, 8-hydroxy-5-deazaflavin (8-HDF), and, flavin adenine dinucleotide (FAD) which, in contrast to the 8-HDF, chromophore, is indispensable for catalytic activity. This work reports, the crystallization and structure at 1.8 A resolution of DNA photolyase, devoid of its 8-HDF chromophore (apophotolyase). The overall, three-dimensional structure is similar to that of the holoenzyme, indicating that the presence of 8-HDF is not essential for the correct, folding of the enzyme. Structural changes include an additional phosphate, group, a different conformation for Arg11 and slight rearrangements of, Met47, Asp101 and Asp382, which replace part of the 8-HDF molecule in the, chromophore-binding pocket. The apophotolyase can be efficiently, reconstituted with synthetic 8-hydroxy-5-deazariboflavin, despite the, orientation of Arg11 and the presence of the phosphate group in the 8-HDF, pocket. Red light or X-rays reduced the FAD chromophore in apophotolyase, crystals, as observed by single-crystal spectrophotometry. The structural, effects of FAD reduction were determined by comparison of three data sets, that were successively collected at 100 K, while the degree of reduction, was monitored online by changes in the light absorption of the crystals., X-ray-induced conformational changes were confined to the active site of, the protein. They include sub-angstrom movements of the O(2) and N(5), atoms of the flavin group as well as the O(delta) atoms of the surrounding, amino acids Asp380 and Asn386.
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<StructureSection load='1owp' size='340' side='right'caption='[[1owp]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[1owp]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Synechococcus_elongatus_PCC_6301 Synechococcus elongatus PCC 6301]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OWP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OWP FirstGlance]. <br>
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1OWP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Synechococcus_sp. Synechococcus sp.] with PO4 and FAD as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Deoxyribodipyrimidine_photo-lyase Deoxyribodipyrimidine photo-lyase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.99.3 4.1.99.3] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1OWP OCA].
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
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==Reference==
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1owp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1owp OCA], [https://pdbe.org/1owp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1owp RCSB], [https://www.ebi.ac.uk/pdbsum/1owp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1owp ProSAT]</span></td></tr>
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DNA apophotolyase from Anacystis nidulans: 1.8 A structure, 8-HDF reconstitution and X-ray-induced FAD reduction., Kort R, Komori H, Adachi S, Miki K, Eker A, Acta Crystallogr D Biol Crystallogr. 2004 Jul;60(Pt 7):1205-13. Epub 2004, Jun 22. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15213381 15213381]
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</table>
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[[Category: Deoxyribodipyrimidine photo-lyase]]
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== Function ==
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[[Category: Single protein]]
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[https://www.uniprot.org/uniprot/PHR_SYNP6 PHR_SYNP6] 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.
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[[Category: Synechococcus sp.]]
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== Evolutionary Conservation ==
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[[Category: Adachi, S.]]
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[[Image:Consurf_key_small.gif|200px|right]]
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[[Category: Eker, A.]]
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Check<jmol>
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[[Category: Komori, H.]]
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<jmolCheckbox>
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[[Category: Kort, R.]]
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ow/1owp_consurf.spt"</scriptWhenChecked>
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[[Category: Miki, K.]]
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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[[Category: FAD]]
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<text>to colour the structure by Evolutionary Conservation</text>
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[[Category: PO4]]
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</jmolCheckbox>
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[[Category: dna repair]]
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</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=1owp ConSurf].
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[[Category: flavin enzyme]]
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<div style="clear:both"></div>
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[[Category: photoreactivating enzyme]]
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__TOC__
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</StructureSection>
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 23:15:26 2007''
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[[Category: Large Structures]]
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[[Category: Synechococcus elongatus PCC 6301]]
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[[Category: Adachi S]]
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[[Category: Eker A]]
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[[Category: Komori H]]
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[[Category: Kort R]]
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[[Category: Miki K]]

Current revision

DATA6:photoreduced DNA pholyase / received X-rays dose 4.8 exp15 photons/mm2

PDB ID 1owp

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