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New page: left|200px<br /><applet load="1dnp" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dnp, resolution 2.3Å" /> '''STRUCTURE OF DEOXYRIB...
 
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[[Image:1dnp.jpg|left|200px]]<br /><applet load="1dnp" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1dnp.jpg|left|200px]]<br /><applet load="1dnp" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1dnp, resolution 2.3&Aring;" />
caption="1dnp, resolution 2.3&Aring;" />
'''STRUCTURE OF DEOXYRIBODIPYRIMIDINE PHOTOLYASE'''<br />
'''STRUCTURE OF DEOXYRIBODIPYRIMIDINE PHOTOLYASE'''<br />


==Overview==
==Overview==
Photolyase repairs ultraviolet (UV) damage to DNA by splitting the, cyclobutane ring of the major UV photoproduct, the cis, syn-cyclobutane, pyrimidine dimer (Pyr &lt;&gt; Pyr). The reaction is initiated by blue light and, proceeds through long-range energy transfer, single electron transfer, and, enzyme catalysis by a radical mechanism. The three-dimensional, crystallographic structure of DNA photolyase from Escherichia coli is, presented and the atomic model was refined to an R value of 0.172 at 2.3 A, resolution. The polypeptide chain of 471 amino acids is folded into an, amino-terminal alpha/beta domain resembling dinucleotide binding domains, and a carboxyl-terminal helical domain; a loop of 72 residues connects the, domains. The light-harvesting cofactor, 5,10-methenyltetrahydrofolylpolyglutamate (MTHF) binds in a cleft between, the two domains. Energy transfer from MTHF to the catalytic cofactor, flavin adenine dinucleotide (FAD) occurs over a distance of 16.8 A. The, FAD adopts a U-shaped conformation between two helix clusters in the, center of the helical domain and is accessible through a hole in the, surface of this domain. Dimensions and polarity of the hole match those of, a Pyr &lt;&gt; Pyr dinucleotide, suggesting that the Pyr &lt;&gt; Pyr "flips out" of, the helix to fit into this hole, and that electron transfer between the, flavin and the Pyr &lt;&gt; Pyr occurs over van der Waals contact distance.
Photolyase repairs ultraviolet (UV) damage to DNA by splitting the cyclobutane ring of the major UV photoproduct, the cis, syn-cyclobutane pyrimidine dimer (Pyr &lt;&gt; Pyr). The reaction is initiated by blue light and proceeds through long-range energy transfer, single electron transfer, and enzyme catalysis by a radical mechanism. The three-dimensional crystallographic structure of DNA photolyase from Escherichia coli is presented and the atomic model was refined to an R value of 0.172 at 2.3 A resolution. The polypeptide chain of 471 amino acids is folded into an amino-terminal alpha/beta domain resembling dinucleotide binding domains and a carboxyl-terminal helical domain; a loop of 72 residues connects the domains. The light-harvesting cofactor 5,10-methenyltetrahydrofolylpolyglutamate (MTHF) binds in a cleft between the two domains. Energy transfer from MTHF to the catalytic cofactor flavin adenine dinucleotide (FAD) occurs over a distance of 16.8 A. The FAD adopts a U-shaped conformation between two helix clusters in the center of the helical domain and is accessible through a hole in the surface of this domain. Dimensions and polarity of the hole match those of a Pyr &lt;&gt; Pyr dinucleotide, suggesting that the Pyr &lt;&gt; Pyr "flips out" of the helix to fit into this hole, and that electron transfer between the flavin and the Pyr &lt;&gt; Pyr occurs over van der Waals contact distance.


==About this Structure==
==About this Structure==
1DNP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with FAD and MHF as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1DNP OCA].  
1DNP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=FAD:'>FAD</scene> and <scene name='pdbligand=MHF:'>MHF</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DNP OCA].  


==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Deisenhofer, J.]]
[[Category: Deisenhofer, J.]]
[[Category: Park, H.W.]]
[[Category: Park, H W.]]
[[Category: Sancar, A.]]
[[Category: Sancar, A.]]
[[Category: FAD]]
[[Category: FAD]]
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[[Category: lyase]]
[[Category: lyase]]


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