1m0e

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(New page: 200px<br /><applet load="1m0e" size="450" color="white" frame="true" align="right" spinBox="true" caption="1m0e, resolution 2.50&Aring;" /> '''ZEBULARINE: A NOVEL ...)
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'''ZEBULARINE: A NOVEL DNA METHYLATION INHIBITOR THAT FORMS A COVALENT COMPLEX WITH DNA METHYLTRANSFERASE'''<br />
'''ZEBULARINE: A NOVEL DNA METHYLATION INHIBITOR THAT FORMS A COVALENT COMPLEX WITH DNA METHYLTRANSFERASE'''<br />
==Overview==
==Overview==
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Mechanism-based inhibitors of enzymes, which mimic reactive intermediates, in the reaction pathway, have been deployed extensively in the analysis of, metabolic pathways and as candidate drugs. The inhibition of, cytosine-[C5]-specific DNA methyltransferases (C5 MTases) by, oligodeoxynucleotides containing 5-azadeoxycytidine (AzadC) and, 5-fluorodeoxycytidine (FdC) provides a well-documented example of, mechanism-based inhibition of enzymes central to nucleic acid metabolism., Here, we describe the interaction between the C5 MTase from Haemophilus, haemolyticus (M.HhaI) and an oligodeoxynucleotide duplex containing 2-H, pyrimidinone, an analogue often referred to as zebularine and known to, give rise to high-affinity complexes with MTases. X-ray crystallography, has demonstrated the formation of a covalent bond between M.HhaI and the, 2-H pyrimidinone-containing oligodeoxynucleotide. This observation enables, a comparison between the mechanisms of action of 2-H pyrimidinone with, other mechanism-based inhibitors such as FdC. This novel complex provides, a molecular explanation for the mechanism of action of the anti-cancer, drug zebularine.
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Mechanism-based inhibitors of enzymes, which mimic reactive intermediates in the reaction pathway, have been deployed extensively in the analysis of metabolic pathways and as candidate drugs. The inhibition of cytosine-[C5]-specific DNA methyltransferases (C5 MTases) by oligodeoxynucleotides containing 5-azadeoxycytidine (AzadC) and 5-fluorodeoxycytidine (FdC) provides a well-documented example of mechanism-based inhibition of enzymes central to nucleic acid metabolism. Here, we describe the interaction between the C5 MTase from Haemophilus haemolyticus (M.HhaI) and an oligodeoxynucleotide duplex containing 2-H pyrimidinone, an analogue often referred to as zebularine and known to give rise to high-affinity complexes with MTases. X-ray crystallography has demonstrated the formation of a covalent bond between M.HhaI and the 2-H pyrimidinone-containing oligodeoxynucleotide. This observation enables a comparison between the mechanisms of action of 2-H pyrimidinone with other mechanism-based inhibitors such as FdC. This novel complex provides a molecular explanation for the mechanism of action of the anti-cancer drug zebularine.
==About this Structure==
==About this Structure==
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1M0E is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Haemophilus_haemolyticus Haemophilus haemolyticus] with SAH as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Deleted_entry Deleted entry], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.73 2.1.1.73] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1M0E OCA].
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1M0E is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Haemophilus_haemolyticus Haemophilus haemolyticus] with <scene name='pdbligand=SAH:'>SAH</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Deleted_entry Deleted entry], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.73 2.1.1.73] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M0E OCA].
==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Cheng, X.]]
[[Category: Cheng, X.]]
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[[Category: Connolly, B.A.]]
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[[Category: Connolly, B A.]]
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[[Category: Dickman, M.J.]]
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[[Category: Dickman, M J.]]
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[[Category: Hornby, D.P.]]
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[[Category: Hornby, D P.]]
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[[Category: Hurd, P.J.]]
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[[Category: Hurd, P J.]]
[[Category: Zhou, L.]]
[[Category: Zhou, L.]]
[[Category: SAH]]
[[Category: SAH]]
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[[Category: zebularine]]
[[Category: zebularine]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 21:01:54 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:50:09 2008''

Revision as of 11:50, 21 February 2008


1m0e, resolution 2.50Å

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ZEBULARINE: A NOVEL DNA METHYLATION INHIBITOR THAT FORMS A COVALENT COMPLEX WITH DNA METHYLTRANSFERASE

Overview

Mechanism-based inhibitors of enzymes, which mimic reactive intermediates in the reaction pathway, have been deployed extensively in the analysis of metabolic pathways and as candidate drugs. The inhibition of cytosine-[C5]-specific DNA methyltransferases (C5 MTases) by oligodeoxynucleotides containing 5-azadeoxycytidine (AzadC) and 5-fluorodeoxycytidine (FdC) provides a well-documented example of mechanism-based inhibition of enzymes central to nucleic acid metabolism. Here, we describe the interaction between the C5 MTase from Haemophilus haemolyticus (M.HhaI) and an oligodeoxynucleotide duplex containing 2-H pyrimidinone, an analogue often referred to as zebularine and known to give rise to high-affinity complexes with MTases. X-ray crystallography has demonstrated the formation of a covalent bond between M.HhaI and the 2-H pyrimidinone-containing oligodeoxynucleotide. This observation enables a comparison between the mechanisms of action of 2-H pyrimidinone with other mechanism-based inhibitors such as FdC. This novel complex provides a molecular explanation for the mechanism of action of the anti-cancer drug zebularine.

About this Structure

1M0E is a Single protein structure of sequence from Haemophilus haemolyticus with as ligand. Active as Deleted entry, with EC number 2.1.1.73 Full crystallographic information is available from OCA.

Reference

Zebularine: a novel DNA methylation inhibitor that forms a covalent complex with DNA methyltransferases., Zhou L, Cheng X, Connolly BA, Dickman MJ, Hurd PJ, Hornby DP, J Mol Biol. 2002 Aug 23;321(4):591-9. PMID:12206775

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