PDBsum entry 2g7h

Transferase

PDB id

2g7h

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Contents

			Protein chain

					167 a.a. *

* Residue conservation analysis

PDB id:

2g7h

Links
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Name:

Transferase

Title:

Structure of an o6-methylguanine DNA methyltransferase from methanococcus jannaschii (mj1529)

Structure:

Methylated-DNA--protein-cysteine methyltransferase. Chain: a. Synonym: 6-o- methylguanine-DNA methyltransferase, mgmt, o-6- methylguanine-DNA- alkyltransferase. Engineered: yes

Source:

Methanocaldococcus jannaschii. Organism_taxid: 2190. Gene: ogt. Expressed in: escherichia coli. Expression_system_taxid: 562.

NMR struc:

10 models

Authors:

A.Roberts

Key ref:

A.Roberts et al. (2006). Structural studies of MJ1529, an O6-methylguanine-DNA methyltransferase. Magn Reson Chem, 44, S71. PubMed id: 16826543

Date:

28-Feb-06

Release date:

01-Aug-06

PROCHECK

	Headers

	References

Protein chain

Q58924 (OGT_METJA) - Methylated-DNA--protein-cysteine methyltransferase from Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)

Seq: Struc:					167 a.a. 167 a.a.

Key:

PfamA domain

Secondary structure

CATH domain



		Enzyme reactions

Enzyme class:

E.C.2.1.1.63 - methylated-DNA--[protein]-cysteine S-methyltransferase.

[IntEnz] [ExPASy] [KEGG] [BRENDA]

Reaction:

1.	a 6-O-methyl-2'-deoxyguanosine in DNA + L-cysteinyl-[protein] = S-methyl-L-cysteinyl-[protein] + a 2'-deoxyguanosine in DNA
2.	a 4-O-methyl-thymidine in DNA + L-cysteinyl-[protein] = a thymidine in DNA + S-methyl-L-cysteinyl-[protein]

DNA (containing 6-O-methylguanine)	+	protein L-cysteine	=	DNA (without 6-O-methylguanine)	+	protein S-methyl-L-cysteine

DNA (containing 4-O-methylthymine)	+	protein L-cysteine	=	DNA (without 4-O-methylthymine)	+	protein S-methyl-L-cysteine

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

reference

	Magn Reson Chem 44:S71 (2006)
PubMed id: 16826543

Structural studies of MJ1529, an O6-methylguanine-DNA methyltransferase.
A.Roberts, J.G.Pelton, D.E.Wemmer.

ABSTRACT

The structure of an O6-methylguanine-DNA methyltransferase (MGMT) from the thermophile Methanococcus jannaschii has been determined using multinuclear multidimensional NMR spectroscopy. The structure is similar to homologs from other organisms that have been determined by crystallography, with some variation in the N-terminal domain. The C-terminal domain is more highly conserved in both sequence and structure. Regions of the protein show broadening, reflecting conformational flexibility that is likely related to function.

Literature references that cite this PDB file's key reference

PubMed id

Reference

18803403

Q.Fang, A.M.Noronha, S.P.Murphy, C.J.Wilds, J.L.Tubbs, J.A.Tainer, G.Chowdhury, F.P.Guengerich, and A.E.Pegg (2008).
Repair of O6-G-alkyl-O6-G interstrand cross-links by human O6-alkylguanine-DNA alkyltransferase.

Biochemistry, 47, 10892-10903.

The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time.