1dct
From Proteopedia
(New page: 200px<br /><applet load="1dct" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dct, resolution 2.800Å" /> '''DNA (CYTOSINE-5) ME...) |
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| - | [[Image:1dct.gif|left|200px]]<br /><applet load="1dct" size=" | + | [[Image:1dct.gif|left|200px]]<br /><applet load="1dct" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1dct, resolution 2.800Å" /> | caption="1dct, resolution 2.800Å" /> | ||
'''DNA (CYTOSINE-5) METHYLASE FROM HAEIII COVALENTLY BOUND TO DNA'''<br /> | '''DNA (CYTOSINE-5) METHYLASE FROM HAEIII COVALENTLY BOUND TO DNA'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Many organisms expand the information content of their genome through | + | Many organisms expand the information content of their genome through enzymatic methylation of cytosine residues. Here we report the 2.8 A crystal structure of a bacterial DNA (cytosine-5)-methyltransferase (DCMtase), M. HaeIII, bound covalently to DNA. In this complex, the substrate cytosine is extruded from the DNA helix and inserted into the active site of the enzyme, as has been observed for another DCMtase, M. HhaI. The DNA is bound in a cleft between the two domains of the protein and is distorted from the characteristic B-form conformation at its recognition sequence. A comparison of structures shows a variation in the mode of DNA recognition: M. HaeIII differs from M. HhaI in that the remaining bases in its recognition sequence undergo an extensive rearrangement in their pairing. In this process, the bases are unstacked, and a gap 8 A long opens in the DNA. |
==About this Structure== | ==About this Structure== | ||
| - | 1DCT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Haemophilus_aegyptius Haemophilus aegyptius] with CA 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:// | + | 1DCT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Haemophilus_aegyptius Haemophilus aegyptius] with <scene name='pdbligand=CA:'>CA</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=1DCT OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Chen, L.]] | [[Category: Chen, L.]] | ||
| - | [[Category: Lipscomb, W | + | [[Category: Lipscomb, W N.]] |
| - | [[Category: Reinisch, K | + | [[Category: Reinisch, K M.]] |
| - | [[Category: Verdine, G | + | [[Category: Verdine, G L.]] |
[[Category: CA]] | [[Category: CA]] | ||
[[Category: cytosine methylase]] | [[Category: cytosine methylase]] | ||
[[Category: enzyme]] | [[Category: enzyme]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:15:21 2008'' |
Revision as of 10:15, 21 February 2008
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DNA (CYTOSINE-5) METHYLASE FROM HAEIII COVALENTLY BOUND TO DNA
Overview
Many organisms expand the information content of their genome through enzymatic methylation of cytosine residues. Here we report the 2.8 A crystal structure of a bacterial DNA (cytosine-5)-methyltransferase (DCMtase), M. HaeIII, bound covalently to DNA. In this complex, the substrate cytosine is extruded from the DNA helix and inserted into the active site of the enzyme, as has been observed for another DCMtase, M. HhaI. The DNA is bound in a cleft between the two domains of the protein and is distorted from the characteristic B-form conformation at its recognition sequence. A comparison of structures shows a variation in the mode of DNA recognition: M. HaeIII differs from M. HhaI in that the remaining bases in its recognition sequence undergo an extensive rearrangement in their pairing. In this process, the bases are unstacked, and a gap 8 A long opens in the DNA.
About this Structure
1DCT is a Single protein structure of sequence from Haemophilus aegyptius with as ligand. Active as Deleted entry, with EC number 2.1.1.73 Full crystallographic information is available from OCA.
Reference
The crystal structure of HaeIII methyltransferase convalently complexed to DNA: an extrahelical cytosine and rearranged base pairing., Reinisch KM, Chen L, Verdine GL, Lipscomb WN, Cell. 1995 Jul 14;82(1):143-53. PMID:7606780
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