1dct
From Proteopedia
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|PDB= 1dct |SIZE=350|CAPTION= <scene name='initialview01'>1dct</scene>, resolution 2.800Å | |PDB= 1dct |SIZE=350|CAPTION= <scene name='initialview01'>1dct</scene>, resolution 2.800Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=CA:CALCIUM ION'>CA</scene> | + | |LIGAND= <scene name='pdbligand=5CM:5-METHYL-2'-DEOXY-CYTIDINE-5'-MONOPHOSPHATE'>5CM</scene>, <scene name='pdbligand=C49:4-THIO,5-FLUORO,5-METHYL-2'-DEOXY-CYTIDINE-5'-MONOPHOSPHATE'>C49</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=DA:2'-DEOXYADENOSINE-5'-MONOPHOSPHATE'>DA</scene>, <scene name='pdbligand=DC:2'-DEOXYCYTIDINE-5'-MONOPHOSPHATE'>DC</scene>, <scene name='pdbligand=DG:2'-DEOXYGUANOSINE-5'-MONOPHOSPHATE'>DG</scene>, <scene name='pdbligand=DT:THYMIDINE-5'-MONOPHOSPHATE'>DT</scene> |
| - | |ACTIVITY= [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] | + | |ACTIVITY= <span class='plainlinks'>[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] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1dct FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dct OCA], [http://www.ebi.ac.uk/pdbsum/1dct PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1dct RCSB]</span> | ||
}} | }} | ||
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[[Category: Reinisch, K M.]] | [[Category: Reinisch, K M.]] | ||
[[Category: Verdine, G L.]] | [[Category: Verdine, G L.]] | ||
| - | [[Category: CA]] | ||
[[Category: cytosine methylase]] | [[Category: cytosine methylase]] | ||
[[Category: enzyme]] | [[Category: enzyme]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:39:08 2008'' |
Revision as of 16:39, 30 March 2008
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| , resolution 2.800Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , , , , , | ||||||
| Activity: | Deleted entry, with EC number 2.1.1.73 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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
Page seeded by OCA on Sun Mar 30 19:39:08 2008
