1yfj

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(New page: 200px<br /><applet load="1yfj" size="450" color="white" frame="true" align="right" spinBox="true" caption="1yfj, resolution 2.69&Aring;" /> '''T4Dam in Complex wit...)
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[[Image:1yfj.gif|left|200px]]<br /><applet load="1yfj" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1yfj.gif|left|200px]]<br /><applet load="1yfj" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1yfj, resolution 2.69&Aring;" />
caption="1yfj, resolution 2.69&Aring;" />
'''T4Dam in Complex with AdoHcy and 15-mer Oligonucleotide Showing Semi-specific and Specific Contact'''<br />
'''T4Dam in Complex with AdoHcy and 15-mer Oligonucleotide Showing Semi-specific and Specific Contact'''<br />
==Overview==
==Overview==
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DNA methyltransferases methylate target bases within specific nucleotide, sequences. Three structures are described for bacteriophage T4 DNA-adenine, methyltransferase (T4Dam) in ternary complexes with partially and fully, specific DNA and a methyl-donor analog. We also report the effects of, substitutions in the related Escherichia coli DNA methyltransferase, (EcoDam), altering residues corresponding to those involved in specific, interaction with the canonical GATC target sequence in T4Dam. We have, identified two types of protein-DNA interactions: discriminatory contacts, which stabilize the transition state and accelerate methylation of the, cognate site, and antidiscriminatory contacts, which do not significantly, affect methylation of the cognate site but disfavor activity at noncognate, sites. These structures illustrate the transition in enzyme-DNA, interaction from nonspecific to specific interaction, suggesting that, there is a temporal order for formation of specific contacts.
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DNA methyltransferases methylate target bases within specific nucleotide sequences. Three structures are described for bacteriophage T4 DNA-adenine methyltransferase (T4Dam) in ternary complexes with partially and fully specific DNA and a methyl-donor analog. We also report the effects of substitutions in the related Escherichia coli DNA methyltransferase (EcoDam), altering residues corresponding to those involved in specific interaction with the canonical GATC target sequence in T4Dam. We have identified two types of protein-DNA interactions: discriminatory contacts, which stabilize the transition state and accelerate methylation of the cognate site, and antidiscriminatory contacts, which do not significantly affect methylation of the cognate site but disfavor activity at noncognate sites. These structures illustrate the transition in enzyme-DNA interaction from nonspecific to specific interaction, suggesting that there is a temporal order for formation of specific contacts.
==About this Structure==
==About this Structure==
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1YFJ 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 CL, CA and SAH as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Site-specific_DNA-methyltransferase_(adenine-specific) Site-specific DNA-methyltransferase (adenine-specific)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.72 2.1.1.72] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1YFJ OCA].
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1YFJ 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=CL:'>CL</scene>, <scene name='pdbligand=CA:'>CA</scene> and <scene name='pdbligand=SAH:'>SAH</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Site-specific_DNA-methyltransferase_(adenine-specific) Site-specific DNA-methyltransferase (adenine-specific)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.72 2.1.1.72] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YFJ OCA].
==Reference==
==Reference==
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[[Category: Cheng, X.]]
[[Category: Cheng, X.]]
[[Category: Hattman, S.]]
[[Category: Hattman, S.]]
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[[Category: Horton, J.R.]]
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[[Category: Horton, J R.]]
[[Category: Jeltsch, A.]]
[[Category: Jeltsch, A.]]
[[Category: Liebert, K.]]
[[Category: Liebert, K.]]
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[[Category: t4dam]]
[[Category: t4dam]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 06:44:18 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:04:47 2008''

Revision as of 14:04, 21 February 2008


1yfj, resolution 2.69Å

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T4Dam in Complex with AdoHcy and 15-mer Oligonucleotide Showing Semi-specific and Specific Contact

Overview

DNA methyltransferases methylate target bases within specific nucleotide sequences. Three structures are described for bacteriophage T4 DNA-adenine methyltransferase (T4Dam) in ternary complexes with partially and fully specific DNA and a methyl-donor analog. We also report the effects of substitutions in the related Escherichia coli DNA methyltransferase (EcoDam), altering residues corresponding to those involved in specific interaction with the canonical GATC target sequence in T4Dam. We have identified two types of protein-DNA interactions: discriminatory contacts, which stabilize the transition state and accelerate methylation of the cognate site, and antidiscriminatory contacts, which do not significantly affect methylation of the cognate site but disfavor activity at noncognate sites. These structures illustrate the transition in enzyme-DNA interaction from nonspecific to specific interaction, suggesting that there is a temporal order for formation of specific contacts.

About this Structure

1YFJ is a Single protein structure of sequence from Bacteriophage t4 with , and as ligands. Active as Site-specific DNA-methyltransferase (adenine-specific), with EC number 2.1.1.72 Full crystallographic information is available from OCA.

Reference

Transition from nonspecific to specific DNA interactions along the substrate-recognition pathway of dam methyltransferase., Horton JR, Liebert K, Hattman S, Jeltsch A, Cheng X, Cell. 2005 May 6;121(3):349-61. PMID:15882618

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