2dpm
From Proteopedia
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|PDB= 2dpm |SIZE=350|CAPTION= <scene name='initialview01'>2dpm</scene>, resolution 1.8Å | |PDB= 2dpm |SIZE=350|CAPTION= <scene name='initialview01'>2dpm</scene>, resolution 1.8Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</scene> | + | |LIGAND= <scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</scene>, <scene name='pdbligand=SAM:S-ADENOSYLMETHIONINE'>SAM</scene> |
| - | |ACTIVITY= [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] | + | |ACTIVITY= <span class='plainlinks'>[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] </span> |
|GENE= DPNM ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1313 Streptococcus pneumoniae]) | |GENE= DPNM ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1313 Streptococcus pneumoniae]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2dpm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2dpm OCA], [http://www.ebi.ac.uk/pdbsum/2dpm PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2dpm RCSB]</span> | ||
}} | }} | ||
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[[Category: Springhorn, S S.]] | [[Category: Springhorn, S S.]] | ||
[[Category: Tran, P H.]] | [[Category: Tran, P H.]] | ||
| - | [[Category: HG]] | ||
| - | [[Category: SAM]] | ||
[[Category: dna adenine methyltransferase]] | [[Category: dna adenine methyltransferase]] | ||
[[Category: dna methyltransferase group alpha]] | [[Category: dna methyltransferase group alpha]] | ||
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[[Category: s-adenosylmethionine]] | [[Category: s-adenosylmethionine]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:37:42 2008'' |
Revision as of 23:37, 30 March 2008
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| , resolution 1.8Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Gene: | DPNM (Streptococcus pneumoniae) | ||||||
| Activity: | Site-specific DNA-methyltransferase (adenine-specific), with EC number 2.1.1.72 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
DPNM DNA ADENINE METHYLTRANSFERASE FROM STREPTOCCOCUS PNEUMONIAE COMPLEXED WITH S-ADENOSYLMETHIONINE
Overview
Background:. Methyltransferases (Mtases) catalyze the transfer of methyl groups from S-adenosylmethionine (AdoMet) to a variety of small molecular and macromolecular substrates. These enzymes contain a characteristic alpha/beta structural fold. Four groups of DNA Mtases have been defined and representative structures have been determined for three groups. DpnM is a DNA Mtase that acts on adenine N6 in the sequence GATC; the enzyme represents group alpha DNA Mtases, for which no structures are known. Results:. The structure of DpnM in complex with AdoMet was determined at 1.80 A resolution. The protein comprises a consensus Mtase fold with a helical cluster insert. DpnM binds AdoMet in a similar manner to most other Mtases and the enzyme contains a hollow that can accommodate DNA. The helical cluster supports a shelf within the hollow that may recognize the target sequence. Modeling studies indicate a potential site for binding the target adenine, everted from the DNA helix. Comparison of the DpnM structure and sequences of group alpha DNA Mtases indicates that the group is a genetically related family. Structural comparisons show DpnM to be most similar to a small-molecule Mtase and then to macromolecular Mtases, although several dehydrogenases show greater similarity than one DNA Mtase. Conclusions:. DpnM, and by extension the DpnM family or group alpha Mtases, contains the consensus fold and AdoMet-binding motifs found in most Mtases. Structural considerations suggest that macromolecular Mtases evolved from small-molecule Mtases, with different groups of DNA Mtases evolving independently. Mtases may have evolved from dehydrogenases. Comparison of these enzymes indicates that in protein evolution, the structural fold is most highly conserved, then function and lastly sequence.
About this Structure
2DPM is a Single protein structure of sequence from Streptococcus pneumoniae. Full crystallographic information is available from OCA.
Reference
Crystal structure of the DpnM DNA adenine methyltransferase from the DpnII restriction system of streptococcus pneumoniae bound to S-adenosylmethionine., Tran PH, Korszun ZR, Cerritelli S, Springhorn SS, Lacks SA, Structure. 1998 Dec 15;6(12):1563-75. PMID:9862809
Page seeded by OCA on Mon Mar 31 02:37:42 2008
Categories: Single protein | Site-specific DNA-methyltransferase (adenine-specific) | Streptococcus pneumoniae | Cerritelli, S. | Korszun, Z R. | Lacks, S A. | Springhorn, S S. | Tran, P H. | Dna adenine methyltransferase | Dna methyltransferase group alpha | Dna n6-adenine methylation | Dpnii restriction-modification system | Gatc methylation | Methylase | Methyltransferase | Rossman fold | S-adenosylmethionine
