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1yfh

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1yfh, resolution 3.01Å ()

Ligands:

Non-Standard Residues:

Gene:

MGMT (Homo sapiens)

Activity:

[protein-cysteine_S-methyltransferase Methylated-DNA--[protein]-cysteine S-methyltransferase], with EC number 2.1.1.63

Domains:

DNA_binding_1, PRK00901, Methyltransf_1N

Structural annotation:
Resources:	CATH : 1Yfha01, 1Yfha02, 1Yfhb01, 1Yfhb02, 1Yfhc01, 1Yfhc02 InterPro : Ipr000169, Ipr011991, Ipr008332, Ipr001497, Ipr014048 Pfam : PF02870, PF01035 UniProt : P16455

Functional annotation:
Resources:	GeneCard : MGMT
Cellular component:	nucleus
Biological process:	DNA repair DNA ligation regulation of caspase activity DNA dealkylation response to DNA damage stimulus
Molecular function:	DNA binding transferase activity methyltransferase activity metal ion binding DNA-methyltransferase activity methylated-DNA-[protein-cysteine S-methyltransferase activity] zinc ion binding

Evolutionary conservation:

Toggle Conservation Colors:

Rows = identical sequences:

Further Information:

Caveats,

Explanation,
Complete Results at ConSurfDB

Resources:

FirstGlance, OCA, PDBsum, RCSB

Coordinates:

save as pdb, mmCIF, xml

wt Human O6-Alkylguanine-DNA Alkyltransferase Bound To DNA Containing an Alkylated Cytosine

Publication Abstract from PubMed

O6-Alklyguanine-DNA alkyltransferase (AGT) is an important DNA repair protein that protects cells from mutagenesis and toxicity arising from alkylating agents. We present an X-ray crystal structure of the wild-type human protein (hAGT) bound to double-stranded DNA with a chemically modified cytosine base. The protein binds at two different sites: one at the modified base, and the other across a sticky-ended DNA junction. The protein molecule that binds the modified cytosine base flips the base and recognizes it in its active site. The one that binds ends of neighboring DNA molecules partially flips an overhanging thymine base. This base is not inserted into the active-site pocket of the protein. These two different hAGT/DNA interactions observed in the structure suggest that hAGT may not detect DNA lesions by searching for the adduct itself, but rather for weakened and/or distorted base-pairs caused by base damage in the duplex DNA. We propose that hAGT imposes a strain on the DNA duplex and searches for DNA regions where the native structure is destabilized. The structure provides implications for pyrimidine recognition, improved inhibitor design, and a possible protein/protein interaction patch on hAGT.

The structure of the human AGT protein bound to DNA and its implications for damage detection., Duguid EM, Rice PA, He C, J Mol Biol. 2005 Jul 22;350(4):657-66. PMID:15964013

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

About this Structure

1YFH is a 7 chains structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Duguid EM, Rice PA, He C. The structure of the human AGT protein bound to DNA and its implications for damage detection. J Mol Biol. 2005 Jul 22;350(4):657-66. PMID:15964013

Page seeded by OCA on Tue Feb 17 20:27:46 2009