1iqr: Difference between revisions
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[[Image:1iqr.jpg|left|200px]] | [[Image:1iqr.jpg|left|200px]] | ||
'''Crystal structure of DNA photolyase from Thermus thermophilus''' | {{Structure | ||
|PDB= 1iqr |SIZE=350|CAPTION= <scene name='initialview01'>1iqr</scene>, resolution 2.1Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene> and <scene name='pdbligand=FAD:FLAVIN-ADENINE DINUCLEOTIDE'>FAD</scene> | |||
|ACTIVITY= [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] | |||
|GENE= | |||
}} | |||
'''Crystal structure of DNA photolyase from Thermus thermophilus''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1IQR is a [ | 1IQR is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IQR OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/11707580 11707580] | ||
[[Category: Deoxyribodipyrimidine photo-lyase]] | [[Category: Deoxyribodipyrimidine photo-lyase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: riken structural genomics/proteomics initiative]] | [[Category: riken structural genomics/proteomics initiative]] | ||
[[Category: rsgi]] | [[Category: rsgi]] | ||
[[Category: structural | [[Category: structural genomic]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:53:38 2008'' | ||
Revision as of 12:53, 20 March 2008
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| , resolution 2.1Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | and | ||||||
| Activity: | Deoxyribodipyrimidine photo-lyase, with EC number 4.1.99.3 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of DNA photolyase from Thermus thermophilus
OverviewOverview
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 StructureAbout this Structure
1IQR is a Single protein structure of sequence from Thermus thermophilus. Full crystallographic information is available from OCA.
ReferenceReference
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
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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)
OCA- Pages with broken file links
- 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.
- FAD
- PO4
- Cyclobutane pyrimidine dimer (cpd)
- Dna repair
- Dna-binding
- Fad
- Photoreactivating enzyme
- Riken structural genomics/proteomics initiative
- Rsgi
- Structural genomic