1iqr

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|PDB= 1iqr |SIZE=350|CAPTION= <scene name='initialview01'>1iqr</scene>, resolution 2.1&Aring;
|PDB= 1iqr |SIZE=350|CAPTION= <scene name='initialview01'>1iqr</scene>, resolution 2.1&Aring;
|SITE=
|SITE=
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|LIGAND= <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene> and <scene name='pdbligand=FAD:FLAVIN-ADENINE DINUCLEOTIDE'>FAD</scene>
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|LIGAND= <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>
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|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]
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|ACTIVITY= <span class='plainlinks'>[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] </span>
|GENE=
|GENE=
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|DOMAIN=
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1iqr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1iqr OCA], [http://www.ebi.ac.uk/pdbsum/1iqr PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1iqr RCSB]</span>
}}
}}
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[[Category: Yokoyama, S.]]
[[Category: Yokoyama, S.]]
[[Category: komori, H.]]
[[Category: komori, H.]]
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[[Category: FAD]]
 
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[[Category: PO4]]
 
[[Category: cyclobutane pyrimidine dimer (cpd)]]
[[Category: cyclobutane pyrimidine dimer (cpd)]]
[[Category: dna repair]]
[[Category: dna repair]]
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[[Category: structural genomic]]
[[Category: structural genomic]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:53:38 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:23:22 2008''

Revision as of 18:23, 30 March 2008


PDB ID 1iqr

Drag the structure with the mouse to rotate
, resolution 2.1Å
Ligands: ,
Activity: Deoxyribodipyrimidine photo-lyase, with EC number 4.1.99.3
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



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

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