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1b5e

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[[Image:1b5e.gif|left|200px]]
[[Image:1b5e.gif|left|200px]]
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{{Structure
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|PDB= 1b5e |SIZE=350|CAPTION= <scene name='initialview01'>1b5e</scene>, resolution 1.60&Aring;
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The line below this paragraph, containing "STRUCTURE_1b5e", creates the "Structure Box" on the page.
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|SITE= <scene name='pdbsite=CAT:The+Sg+Atom+Of+CYS+148+Has+Dual+conform.'>CAT</scene>
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|LIGAND= <scene name='pdbligand=DCM:2&#39;-DEOXYCYTIDINE-5&#39;-MONOPHOSPHATE'>DCM</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[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] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE=
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|DOMAIN=
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{{STRUCTURE_1b5e| PDB=1b5e | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1b5e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1b5e OCA], [http://www.ebi.ac.uk/pdbsum/1b5e PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1b5e RCSB]</span>
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'''DCMP HYDROXYMETHYLASE FROM T4'''
'''DCMP HYDROXYMETHYLASE FROM T4'''
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[[Category: Song, H K.]]
[[Category: Song, H K.]]
[[Category: Suh, S W.]]
[[Category: Suh, S W.]]
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[[Category: dntp synthesizing complex]]
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[[Category: Dntp synthesizing complex]]
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[[Category: hydroxymethylase]]
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[[Category: Hydroxymethylase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 11:05:38 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:53:56 2008''
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Revision as of 08:05, 2 May 2008

Template:STRUCTURE 1b5e

DCMP HYDROXYMETHYLASE FROM T4


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.

About this Structure

1B5E is a Single protein structure of sequence from Enterobacteria phage t4. Full crystallographic information is available from OCA.

Reference

Crystal structure of deoxycytidylate hydroxymethylase from bacteriophage T4, a component of the deoxyribonucleoside triphosphate-synthesizing complex., Song HK, Sohn SH, Suh SW, EMBO J. 1999 Mar 1;18(5):1104-13. PMID:10064578 Page seeded by OCA on Fri May 2 11:05:38 2008

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