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| - | [[Image:1b49.gif|left|200px]] | + | {{Seed}} |
| | + | [[Image:1b49.png|left|200px]] |
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| | {{STRUCTURE_1b49| PDB=1b49 | SCENE= }} | | {{STRUCTURE_1b49| PDB=1b49 | SCENE= }} |
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| - | '''DCMP HYDROXYMETHYLASE FROM T4 (PHOSPHATE-BOUND)'''
| + | ===DCMP HYDROXYMETHYLASE FROM T4 (PHOSPHATE-BOUND)=== |
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| - | ==Overview==
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| - | 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.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_10064578}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 10064578 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_10064578}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Dntp synthesizing complex]] | | [[Category: Dntp synthesizing complex]] |
| | [[Category: Hydroxymethylase]] | | [[Category: Hydroxymethylase]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 11:02:56 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 18:13:12 2008'' |
Revision as of 15:13, 30 June 2008
Template:STRUCTURE 1b49
DCMP HYDROXYMETHYLASE FROM T4 (PHOSPHATE-BOUND)
Template:ABSTRACT PUBMED 10064578
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 Mon Jun 30 18:13:12 2008
