2vtb: Difference between revisions
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< | ==Structure of cryptochrome 3 - DNA complex== | ||
<StructureSection load='2vtb' size='340' side='right'caption='[[2vtb]], [[Resolution|resolution]] 2.01Å' scene=''> | |||
You may | == Structural highlights == | ||
or the | <table><tr><td colspan='2'>[[2vtb]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana] and [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VTB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VTB 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]] 2.01Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=MHF:5,10-METHENYL-6,7,8-TRIHYDROFOLIC+ACID'>MHF</scene>, <scene name='pdbligand=TCP:5-METHYLTHYMIDINE'>TCP</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=2vtb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vtb OCA], [https://pdbe.org/2vtb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vtb RCSB], [https://www.ebi.ac.uk/pdbsum/2vtb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vtb ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/CRYD_ARATH CRYD_ARATH] May have a photoreceptor function. Binds ss- and ds-DNA in a sequence non-specific manner. Has a photolyase activity specific for cyclobutane pyrimidine dimers in ssDNA.<ref>PMID:17062752</ref> | |||
== 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/vt/2vtb_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=2vtb ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
DNA photolyases and cryptochromes (cry) form a family of flavoproteins that use light energy in the blue/UV-A region for the repair of UV-induced DNA lesions or for signaling, respectively. Very recently, it was shown that members of the DASH cryptochrome subclade repair specifically cyclobutane pyrimidine dimers (CPDs) in UV-damaged single-stranded DNA. Here, we report the crystal structure of Arabidopsis cryptochrome 3 with an in-situ-repaired CPD substrate in single-stranded DNA. The structure shows a binding mode similar to that of conventional DNA photolyases. Furthermore, CPD lesions in double-stranded DNA are bound and repaired with similar efficiency as in single-stranded DNA if the CPD lesion is present in a loop structure. Together, these data reveal that DASH cryptochromes catalyze light-driven DNA repair like conventional photolyases but lack an efficient flipping mechanism for interaction with CPD lesions within duplex DNA. | |||
Recognition and repair of UV lesions in loop structures of duplex DNA by DASH-type cryptochrome.,Pokorny R, Klar T, Hennecke U, Carell T, Batschauer A, Essen LO Proc Natl Acad Sci U S A. 2008 Dec 30;105(52):21023-7. Epub 2008 Dec 12. PMID:19074258<ref>PMID:19074258</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2vtb" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Cryptochrome 3D structures|Cryptochrome 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | |||
[[ | |||
== | |||
< | |||
[[Category: Arabidopsis thaliana]] | [[Category: Arabidopsis thaliana]] | ||
[[Category: | [[Category: Homo sapiens]] | ||
[[Category: Batschauer | [[Category: Large Structures]] | ||
[[Category: Carell | [[Category: Batschauer A]] | ||
[[Category: Essen | [[Category: Carell T]] | ||
[[Category: Hennecke | [[Category: Essen L-O]] | ||
[[Category: Klar | [[Category: Hennecke U]] | ||
[[Category: Pokorny | [[Category: Klar T]] | ||
[[Category: Pokorny R]] | |||
Latest revision as of 18:31, 13 December 2023
Structure of cryptochrome 3 - DNA complexStructure of cryptochrome 3 - DNA complex
Structural highlights
FunctionCRYD_ARATH May have a photoreceptor function. Binds ss- and ds-DNA in a sequence non-specific manner. Has a photolyase activity specific for cyclobutane pyrimidine dimers in ssDNA.[1] Evolutionary Conservation![]() Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedDNA photolyases and cryptochromes (cry) form a family of flavoproteins that use light energy in the blue/UV-A region for the repair of UV-induced DNA lesions or for signaling, respectively. Very recently, it was shown that members of the DASH cryptochrome subclade repair specifically cyclobutane pyrimidine dimers (CPDs) in UV-damaged single-stranded DNA. Here, we report the crystal structure of Arabidopsis cryptochrome 3 with an in-situ-repaired CPD substrate in single-stranded DNA. The structure shows a binding mode similar to that of conventional DNA photolyases. Furthermore, CPD lesions in double-stranded DNA are bound and repaired with similar efficiency as in single-stranded DNA if the CPD lesion is present in a loop structure. Together, these data reveal that DASH cryptochromes catalyze light-driven DNA repair like conventional photolyases but lack an efficient flipping mechanism for interaction with CPD lesions within duplex DNA. Recognition and repair of UV lesions in loop structures of duplex DNA by DASH-type cryptochrome.,Pokorny R, Klar T, Hennecke U, Carell T, Batschauer A, Essen LO Proc Natl Acad Sci U S A. 2008 Dec 30;105(52):21023-7. Epub 2008 Dec 12. PMID:19074258[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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