1iqr
From Proteopedia
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'''Crystal structure of DNA photolyase from Thermus thermophilus''' | '''Crystal structure of DNA photolyase from Thermus thermophilus''' | ||
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[[Category: Shibata, T.]] | [[Category: Shibata, T.]] | ||
[[Category: Yokoyama, S.]] | [[Category: Yokoyama, S.]] | ||
| - | [[Category: | + | [[Category: Komori, H.]] |
| - | [[Category: | + | [[Category: Dna repair]] |
| - | + | [[Category: Dna-binding]] | |
| - | [[Category: | + | [[Category: Fad]] |
| - | [[Category: | + | [[Category: Photoreactivating enzyme]] |
| - | [[Category: | + | [[Category: Riken structural genomics/proteomics initiative]] |
| - | [[Category: | + | [[Category: Rsgi]] |
| - | [[Category: | + | [[Category: Structural genomic]] |
| - | [[Category: | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 20:17:44 2008'' |
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Revision as of 17:17, 2 May 2008
Crystal structure of DNA photolyase from Thermus thermophilus
Overview
DNA photolyase is a pyrimidine-dimer repair enzyme that uses visible light. Photolyase generally contains two chromophore cofactors. One is a catalytic cofactor directly contributing to the repair of a pyrimidine-dimer. The other is a light-harvesting cofactor, which absorbs visible light and transfers energy to the catalytic cofactor. Photolyases are classified according to their second cofactor into either a folate- or deazaflavin-type. The native structures of both types of photolyases have already been determined, but the mechanism of substrate recognition remains largely unclear because of the lack of structural information regarding the photolyase-substrate complex. Photolyase from Thermus thermophilus, the first thermostable class I photolyase found, is favorable for function analysis, but even the type of the second cofactor has not been identified. Here, we report the crystal structures of T. thermophilus photolyase in both forms of the native enzyme and the complex along with a part of its substrate, thymine. A structural comparison with other photolyases suggests that T. thermophilus photolyase has structural features allowing for thermostability and that its light-harvesting cofactor binding site bears a close resemblance to a deazaflavin-type photolyase. One thymine base is found at the hole, a putative substrate-binding site near the catalytic cofactor in the complex form. This structural data for the photolyase-thymine complex allow us to propose a detailed model for the pyrimidine-dimer recognition mechanism.
About this Structure
1IQR is a Single protein structure of sequence from Thermus thermophilus. Full crystallographic information is available from OCA.
Reference
Crystal structure of thermostable DNA photolyase: pyrimidine-dimer recognition mechanism., Komori H, Masui R, Kuramitsu S, Yokoyama S, Shibata T, Inoue Y, Miki K, Proc Natl Acad Sci U S A. 2001 Nov 20;98(24):13560-5. Epub 2001 Nov 13. PMID:11707580 Page seeded by OCA on Fri May 2 20:17:44 2008
Categories: Deoxyribodipyrimidine photo-lyase | Single protein | Thermus thermophilus | Inoue, Y. | Kuramitsu, S. | Masui, R. | Miki, K. | RSGI, RIKEN Structural Genomics/Proteomics Initiative. | Shibata, T. | Yokoyama, S. | Komori, H. | Dna repair | Dna-binding | Fad | Photoreactivating enzyme | Riken structural genomics/proteomics initiative | Rsgi | Structural genomic
