1b49

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[[Image:1b49.gif|left|200px]]
[[Image:1b49.gif|left|200px]]
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{{Structure
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|PDB= 1b49 |SIZE=350|CAPTION= <scene name='initialview01'>1b49</scene>, resolution 2.30&Aring;
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The line below this paragraph, containing "STRUCTURE_1b49", creates the "Structure Box" on the page.
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|SITE=
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|LIGAND= <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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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{{STRUCTURE_1b49| PDB=1b49 | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1b49 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1b49 OCA], [http://www.ebi.ac.uk/pdbsum/1b49 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1b49 RCSB]</span>
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'''DCMP HYDROXYMETHYLASE FROM T4 (PHOSPHATE-BOUND)'''
'''DCMP HYDROXYMETHYLASE FROM T4 (PHOSPHATE-BOUND)'''
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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 11:02:56 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:53:15 2008''
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Revision as of 08:02, 2 May 2008

Image:1b49.gif

Template:STRUCTURE 1b49

DCMP HYDROXYMETHYLASE FROM T4 (PHOSPHATE-BOUND)


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

1B49 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 11:02:56 2008

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