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1hmy

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(New page: 200px<br /><applet load="1hmy" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hmy, resolution 2.5&Aring;" /> '''CRYSTAL STRUCTURE OF ...)
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[[Image:1hmy.jpg|left|200px]]<br /><applet load="1hmy" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1hmy, resolution 2.5&Aring;" />
caption="1hmy, resolution 2.5&Aring;" />
'''CRYSTAL STRUCTURE OF THE HHAL DNA METHYLTRANSFERASE COMPLEXED WITH S-ADENOSYL-L-METHIONINE'''<br />
'''CRYSTAL STRUCTURE OF THE HHAL DNA METHYLTRANSFERASE COMPLEXED WITH S-ADENOSYL-L-METHIONINE'''<br />
==Overview==
==Overview==
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The first three-dimensional structure of a DNA methyltransferase is, presented. The crystal structure of the DNA, (cytosine-5)-methyltransferase, M.HhaI (recognition sequence: GCGC), complexed with S-adenosyl-L-methionine has been determined and refined at, 2.5 A resolution. The core of the structure is dominated by sequence, motifs conserved among all DNA (cytosine-5)-methyltransferases, and these, are responsible for cofactor binding and methyltransferase function.
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The first three-dimensional structure of a DNA methyltransferase is presented. The crystal structure of the DNA (cytosine-5)-methyltransferase, M.HhaI (recognition sequence: GCGC), complexed with S-adenosyl-L-methionine has been determined and refined at 2.5 A resolution. The core of the structure is dominated by sequence motifs conserved among all DNA (cytosine-5)-methyltransferases, and these are responsible for cofactor binding and methyltransferase function.
==About this Structure==
==About this Structure==
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1HMY 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 SAM as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/DNA_(cytosine-5-)-methyltransferase DNA (cytosine-5-)-methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.37 2.1.1.37] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1HMY OCA].
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1HMY 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=SAM:'>SAM</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/DNA_(cytosine-5-)-methyltransferase DNA (cytosine-5-)-methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.37 2.1.1.37] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HMY OCA].
==Reference==
==Reference==
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[[Category: transferase(methyltransferase)]]
[[Category: transferase(methyltransferase)]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 16:39:45 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:02:58 2008''

Revision as of 11:02, 21 February 2008


1hmy, resolution 2.5Å

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CRYSTAL STRUCTURE OF THE HHAL DNA METHYLTRANSFERASE COMPLEXED WITH S-ADENOSYL-L-METHIONINE

Overview

The first three-dimensional structure of a DNA methyltransferase is presented. The crystal structure of the DNA (cytosine-5)-methyltransferase, M.HhaI (recognition sequence: GCGC), complexed with S-adenosyl-L-methionine has been determined and refined at 2.5 A resolution. The core of the structure is dominated by sequence motifs conserved among all DNA (cytosine-5)-methyltransferases, and these are responsible for cofactor binding and methyltransferase function.

About this Structure

1HMY is a Single protein structure of sequence from Haemophilus haemolyticus with as ligand. Active as DNA (cytosine-5-)-methyltransferase, with EC number 2.1.1.37 Full crystallographic information is available from OCA.

Reference

Crystal structure of the HhaI DNA methyltransferase complexed with S-adenosyl-L-methionine., Cheng X, Kumar S, Posfai J, Pflugrath JW, Roberts RJ, Cell. 1993 Jul 30;74(2):299-307. PMID:8343957

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