1b5d: Difference between revisions

New page: left|200px<br /><applet load="1b5d" size="450" color="white" frame="true" align="right" spinBox="true" caption="1b5d, resolution 2.20Å" /> '''DCMP Hydroxymethylas...
 
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caption="1b5d, resolution 2.20&Aring;" />
caption="1b5d, resolution 2.20&Aring;" />
'''DCMP Hydroxymethylase from T4 (Intact)'''<br />
'''DCMP Hydroxymethylase from T4 (Intact)'''<br />


==Overview==
==Overview==
Bacteriophage T4 deoxycytidylate hydroxymethylase (EC 2.1.2.8), a, homodimer of 246-residue subunits, catalyzes hydroxymethylation of the, cytosine base in deoxycytidylate (dCMP) to produce 5-hydroxymethyl-dCMP., It forms part of a phage DNA protection system and appears to function in, vivo as a component of a multienzyme complex called deoxyribonucleoside, triphosphate (dNTP) synthetase. We have determined its crystal structure, in the presence of the substrate dCMP at 1.6 A resolution. The structure, reveals a subunit fold and a dimerization pattern in common with, thymidylate synthases, despite low (approximately 20%) sequence identity., Among the residues that form the dCMP binding site, those interacting with, the sugar and phosphate are arranged in a configuration similar to the, deoxyuridylate binding site of thymidylate synthases. However, the, residues interacting directly or indirectly with the cytosine base show a, more divergent structure and the presumed folate cofactor binding site is, more open. Our structure reveals a water molecule properly positioned near, C-6 of cytosine to add to the C-7 methylene intermediate during the last, step of hydroxymethylation. On the basis of sequence comparison and, crystal packing analysis, a hypothetical model for the interaction between, T4 deoxycytidylate hydroxymethylase and T4 thymidylate synthase in the, dNTP-synthesizing complex has been built.
Bacteriophage T4 deoxycytidylate hydroxymethylase (EC 2.1.2.8), a homodimer of 246-residue subunits, catalyzes hydroxymethylation of the cytosine base in deoxycytidylate (dCMP) to produce 5-hydroxymethyl-dCMP. It forms part of a phage DNA protection system and appears to function in vivo as a component of a multienzyme complex called deoxyribonucleoside triphosphate (dNTP) synthetase. We have determined its crystal structure in the presence of the substrate dCMP at 1.6 A resolution. The structure reveals a subunit fold and a dimerization pattern in common with thymidylate synthases, despite low (approximately 20%) sequence identity. Among the residues that form the dCMP binding site, those interacting with the sugar and phosphate are arranged in a configuration similar to the deoxyuridylate binding site of thymidylate synthases. However, the residues interacting directly or indirectly with the cytosine base show a more divergent structure and the presumed folate cofactor binding site is more open. Our structure reveals a water molecule properly positioned near C-6 of cytosine to add to the C-7 methylene intermediate during the last step of hydroxymethylation. On the basis of sequence comparison and crystal packing analysis, a hypothetical model for the interaction between T4 deoxycytidylate hydroxymethylase and T4 thymidylate synthase in the dNTP-synthesizing complex has been built.


==About this Structure==
==About this Structure==
1B5D is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacteriophage_t4 Bacteriophage t4] with DCM as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Deoxycytidylate_5-hydroxymethyltransferase Deoxycytidylate 5-hydroxymethyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.2.8 2.1.2.8] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1B5D OCA].  
1B5D is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacteriophage_t4 Bacteriophage t4] with <scene name='pdbligand=DCM:'>DCM</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Deoxycytidylate_5-hydroxymethyltransferase Deoxycytidylate 5-hydroxymethyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.2.8 2.1.2.8] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1B5D OCA].  


==Reference==
==Reference==
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[[Category: Deoxycytidylate 5-hydroxymethyltransferase]]
[[Category: Deoxycytidylate 5-hydroxymethyltransferase]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Sohn, S.H.]]
[[Category: Sohn, S H.]]
[[Category: Song, H.K.]]
[[Category: Song, H K.]]
[[Category: Suh, S.W.]]
[[Category: Suh, S W.]]
[[Category: DCM]]
[[Category: DCM]]
[[Category: dntp synthesizing complex]]
[[Category: dntp synthesizing complex]]
[[Category: hydroxymethylase]]
[[Category: hydroxymethylase]]


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