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2VTB

Structure of cryptochrome 3 - DNA complex

Summary for 2VTB
Entry DOI10.2210/pdb2vtb/pdb
DescriptorCRYPTOCHROME DASH, 5'-D(*DT*DT*DT*DT*DTP)-3', FLAVIN-ADENINE DINUCLEOTIDE, ... (8 entities in total)
Functional Keywordslyase-dna complex, lyase dna complex, flavin adenine dinucleotide, dna, dna-binding, cryptochrome, flavoprotein, mitochondrion, fad, photolyase, chromophore, chloroplast, transit peptide, single-stranded dna, cyclobutane-pyrimidine dimer, lyase/dna
Biological sourceARABIDOPSIS THALIANA (MOUSE-EAR CRESS)
More
Total number of polymer chains12
Total formula weight378972.71
Authors
Pokorny, R.,Klar, T.,Hennecke, U.,Carell, T.,Batschauer, A.,Essen, L.-O. (deposition date: 2008-05-13, release date: 2009-06-02, Last modification date: 2023-12-13)
Primary citationPokorny, R.,Klar, T.,Hennecke, U.,Carell, T.,Batschauer, A.,Essen, L.-O.
Recognition and Repair of Uv Lesions in Loop Structures of Duplex DNA by Dash-Type Cryptochrome.
Proc.Natl.Acad.Sci.USA, 105:21023-, 2008
Cited by
PubMed Abstract: 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.
PubMed: 19074258
DOI: 10.1073/PNAS.0805830106
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.01 Å)
Structure validation

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数据于2025-11-19公开中

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