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1mgt

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[[Image:1mgt.gif|left|200px]]
[[Image:1mgt.gif|left|200px]]
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{{Structure
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|PDB= 1mgt |SIZE=350|CAPTION= <scene name='initialview01'>1mgt</scene>, resolution 1.8&Aring;
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The line below this paragraph, containing "STRUCTURE_1mgt", creates the "Structure Box" on the page.
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|SITE=
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Methylated-DNA--[protein]-cysteine_S-methyltransferase Methylated-DNA--[protein]-cysteine S-methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.63 2.1.1.63] </span>
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{{STRUCTURE_1mgt| PDB=1mgt | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1mgt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mgt OCA], [http://www.ebi.ac.uk/pdbsum/1mgt PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1mgt RCSB]</span>
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'''CRYSTAL STRUCTURE OF O6-METHYLGUANINE-DNA METHYLTRANSFERASE FROM HYPERTHERMOPHILIC ARCHAEON PYROCOCCUS KODAKARAENSIS STRAIN KOD1'''
'''CRYSTAL STRUCTURE OF O6-METHYLGUANINE-DNA METHYLTRANSFERASE FROM HYPERTHERMOPHILIC ARCHAEON PYROCOCCUS KODAKARAENSIS STRAIN KOD1'''
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==Reference==
==Reference==
Hyperthermostable protein structure maintained by intra and inter-helix ion-pairs in archaeal O6-methylguanine-DNA methyltransferase., Hashimoto H, Inoue T, Nishioka M, Fujiwara S, Takagi M, Imanaka T, Kai Y, J Mol Biol. 1999 Sep 24;292(3):707-16. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10497033 10497033]
Hyperthermostable protein structure maintained by intra and inter-helix ion-pairs in archaeal O6-methylguanine-DNA methyltransferase., Hashimoto H, Inoue T, Nishioka M, Fujiwara S, Takagi M, Imanaka T, Kai Y, J Mol Biol. 1999 Sep 24;292(3):707-16. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10497033 10497033]
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[[Category: Methylated-DNA--[protein]-cysteine S-methyltransferase]]
 
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Thermococcus kodakarensis]]
[[Category: Thermococcus kodakarensis]]
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[[Category: Nishioka, M.]]
[[Category: Nishioka, M.]]
[[Category: Takagi, M.]]
[[Category: Takagi, M.]]
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[[Category: dna repair protein]]
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[[Category: Dna repair protein]]
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[[Category: hyperthermostability]]
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[[Category: Hyperthermostability]]
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[[Category: methyltransferase]]
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[[Category: Methyltransferase]]
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[[Category: suicidal enzyme]]
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[[Category: Suicidal enzyme]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 01:00:17 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:15:50 2008''
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Revision as of 22:00, 2 May 2008

Image:1mgt.gif

Template:STRUCTURE 1mgt

CRYSTAL STRUCTURE OF O6-METHYLGUANINE-DNA METHYLTRANSFERASE FROM HYPERTHERMOPHILIC ARCHAEON PYROCOCCUS KODAKARAENSIS STRAIN KOD1


Overview

The crystal structure of O6-methylguanine-DNA methyltransferase (EC 2.1.1.63) of hyperthermophilic archaeon Pyrococcuskodakaraensis strain KOD1 (Pk -MGMT) was determined by single isomorphous replacement method with anomalous scattering (SIRAS) at 1.8 A resolution. The archaeal protein is extremely thermostable and repairs alkylated DNA by suicidal alkyl transfer from guanine O6 to its own cysteine residue. Archaea constitute the third primary kingdom of living organisms, sharing characteristics with procaryotic and eucaryotic cells. They live in various extreme environments and are thought to include the most ancient organisms on the earth. Structural studies on hyperthermophilic archaeal proteins reveal the structural features essential for stability under the extreme environments in which these organisms live, and will provide the structural basis required for stabilizing various mesophilic proteins for industrial applications. Here, we report the crystal structure of Pk-MGMT and structural comparison of Pk-MGMT and methyltransferase homologue from Escherichia coli (AdaC, C-terminal fragment of Ada protein). Analyses of solvent-accessible surface area (SASA) reveals a large discrepancy between Pk-MGMT and AdaC with respect to the property of the ASA. In the Pk-MGMT structure, the intra-helix ion-pairs contribute to reinforce stability of alpha-helices. The inter-helix ion-pairs exist in the interior of Pk-MGMT and stabilize internal packing of tertiary structure. Furthermore, structural features of helix cappings, intra and inter-helix ion-pairs are found around the active-site structure in Pk-MGMT.

About this Structure

1MGT is a Single protein structure of sequence from Thermococcus kodakarensis. Full crystallographic information is available from OCA.

Reference

Hyperthermostable protein structure maintained by intra and inter-helix ion-pairs in archaeal O6-methylguanine-DNA methyltransferase., Hashimoto H, Inoue T, Nishioka M, Fujiwara S, Takagi M, Imanaka T, Kai Y, J Mol Biol. 1999 Sep 24;292(3):707-16. PMID:10497033 Page seeded by OCA on Sat May 3 01:00:17 2008

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