PDBsum entry 4zye

Transferase

PDB id: 4zye

Contents

Protein chain

152 a.a.

Ligands

GOL ×2

NO3 ×3

Waters ×211

PDB id:

4zye

Name:

Transferase

Title:

Crystal structure of sulfolobus solfataricus o6-methylguanine methyltransferase

Structure:

Methylated-DNA--protein-cysteine methyltransferase. Chain: a. Synonym: 6-o-methylguanine-DNA methyltransferase,mgmt,o-6- methylguanine-DNA-alkyltransferase. Engineered: yes. Other_details: proline residue before start methionine was inserted in sub-cloning experiment.

Source:

Sulfolobus solfataricus (strain atcc 35092 / dsm 1617 / jcm 11322 / p2). Organism_taxid: 273057. Strain: atcc 35092 / dsm 1617 / jcm 11322 / p2. Gene: ogt, sso2487. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.

Resolution:

1.85Å R-factor: 0.161 R-free: 0.182

Authors:

R.Miggiano,F.Rossi,M.Rizzi

Key ref:

G.Perugino et al. (2015). Structure-function relationships governing activity and stability of a DNA alkylation damage repair thermostable protein. Nucleic Acids Res, 43, 8801-8816. PubMed id: 26227971 DOI: 10.1093/nar/gkv774

Date:

21-May-15 Release date: 12-Aug-15

Protein chain

Q97VW7  (OGT_SULSO) -  Methylated-DNA--protein-cysteine methyltransferase from Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)

Seq: 151 a.a.

Struc: 152 a.a.

Enzyme reactions

• Enzyme class: E.C.2.1.1.63 - methylated-DNA--[protein]-cysteine S-methyltransferase.
• 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]

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

reference

DOI no: 10.1093/nar/gkv774

Nucleic Acids Res 43:8801-8816 (2015)

PubMed id: 26227971

Structure-function relationships governing activity and stability of a DNA alkylation damage repair thermostable protein.

G.Perugino, R.Miggiano, M.Serpe, A.Vettone, A.Valenti, S.Lahiri, F.Rossi, M.Rossi, M.Rizzi, M.Ciaramella.

ABSTRACT

Alkylated DNA-protein alkyltransferases repair alkylated DNA bases, which are among the most common DNA lesions, and are evolutionary conserved, from prokaryotes to higher eukaryotes. The human ortholog, hAGT, is involved in resistance to alkylating chemotherapy drugs. We report here on the alkylated DNA-protein alkyltransferase, SsOGT, from an archaeal species living at high temperature, a condition that enhances the harmful effect of DNA alkylation. The exceptionally high stability of SsOGT gave us the unique opportunity to perform structural and biochemical analysis of a protein of this class in its post-reaction form. This analysis, along with those performed on SsOGT in its ligand-free and DNA-bound forms, provides insights in the structure-function relationships of the protein before, during and after DNA repair, suggesting a molecular basis for DNA recognition, catalytic activity and protein post-reaction fate, and giving hints on the mechanism of alkylation-induced inactivation of this class of proteins.